Methods of producing polyketide synthase mutants and compositions and uses thereof

ABSTRACT

The present invention comprises crystalline polyketide synthases, isolated non-native polyketide synthases having the structural coordinates of said crystalline polyketide synthases, and nucleic acids encoding such non-native polyketide synthases. Also disclosed are methods of producing mutant polyketide synthases, and methods of altering the activity and/or substrate specificity of putative polyketide synthases.

STATEMENT OF GOVERNMENT SUPPORT

This work is supported in part by grant numbers MCB-9982586 from theNational Science Foundation. The Government has certain rights to thisinvention.

FIELD OF THE INVENTION

The present invention relates to methods for producing mutant polyketidesynthases, and for altering the activity and/or substrate specificity ofputative native and mutant polyketide synthases. The present inventionfurther relates to compositions and uses of mutant polyketide synthases.

BACKGROUND

Advances in molecular biology have allowed the development of biologicalagents useful in modulating protein or nucleic acid activity orexpression, respectively. Many of these advances are based onidentifying the primary sequence of the molecule to be modulated. Forexample, determining the nucleic acid sequence of DNA or RNA allows thedevelopment of antisense or ribozyme molecules. Similarly, identifyingthe primary sequence allows for the identification of sequences that maybe useful in creating monoclonal antibodies. However, often the primarysequence of a protein is insufficient to develop therapeutic ordiagnostic molecules due to the secondary, tertiary or quartenarystructure of the protein from which the primary sequence is obtained.The process of designing potent and specific inhibitors or activatorshas improved with the arrival of techniques for determining thethree-dimensional structure of an enzyme or polypeptide to be modulated.

The phenylpropanoid synthetic pathway in plants produces a class ofcompounds know as anthocyanins, which are used for a variety ofapplications. Anthocyanins are involved in pigmentation and protectionagainst UV photodamage, synthesis of anti-microbial phytoalexins, andare flavonoid inducers of Rhizobium modulation genes 1-4. As medicinalnatural products, the phenylpropanoids exhibit cancer chemopreventiveactivity, as well as anti-mitotic, estrogenic, anti-malarial,anti-oxidant, and antiasthmatic activities. The benefits of consumingred wine, which contains significant amounts of3,4′,5-trihydroxystilbene (resveratrol) and other phenylpropanoids,highlight the dietary importance of these compounds. Chalcone synthase(CHS), a polyketide synthase, plays an essential role in thebiosynthesis of plant phenylpropanoids.

An improvement in the understanding of the structure/function of theseenzymes would allow for the exploitation of the synthetic capabilitiesof known enzymes for production of useful new chemical compounds, orallow for the creation of novel non-native enzymes having new syntheticcapabilities. A need exists, therefore, for a detailed understanding ofthe molecular basis of the chemical reactions involved in polyketidesynthesis. The present invention addresses this and related needs.

SUMMARY OF THE INVENTION

In accordance with the present invention there are presented crystallinepolyketide synthases and the three-dimensional coordinates derivedtherefrom. Three-dimensional coordinates have been obtained for anactive form of chalcone synthase and several active and inactive mutantsthereof, both with and without substrate or substrate analog. Similarresults have been obtained for the polyketide synthases stilbenesynthase (STS) and pyrone synthase (2-PS).

One aspect of the present invention that is made possible by resultsdescribed herein is that the three-dimensional properties of polyketidesynthase proteins are determined, in particular the three-dimensionalproperties of the active site. The invention features specificcoordinates of at least fourteen α carbon atoms defined for the activesite in three-dimensional space. R-groups attached to said α-carbons aredefined such that mutants can be made by changing at least one R-groupfound in the synthase active site. Such mutants may have unique anduseful properties. Thus, in another embodiment of the invention, thereare provided isolated non-native (e.g., mutant) synthase(s) having atleast fourteen active site α-carbons having the structural coordinatesdisclosed herein (see, for example Table 1) and one or more R-groupsother than those found in native polyketide synthase(s).

The three-dimensional coordinates disclosed herein can be employed in avariety of methods. The polyketide synthase used in the crystallizationstudies disclosed herein is a chalcone synthase derived from Medicagosataiva (alfalfa). A large number of proteins have been isolated andsequenced which have primary amino acid sequence similar to that ofchalcone synthase, but for which substrate specificity and/or product isunknown. Thus, in another embodiment of the present invention, there areprovided methods for altering the activity and/or substrate specificityof a putative polyketide synthase. There are further provided methodsfor altering the polyketide content of a plant.

Other aspects, embodiments, advantages, and features of the presentinvention will become apparent from the following specification.

BRIEF DESCRIPTION OF FIGURES

FIG. 1 presents the chemical structures of chalcone, naringenin,resveratrol, and cerulenin.

FIG. 2 presents final SIGMAA-weighted 2Fo-Fc electron density map of theCHS-resveratrol complex in the vicinity of the resveratrol binding site.The map is contoured at 1σ.

FIG. 3 shows a ribbon representation of the CHS homodimer. Theapproximate alpha carbon positions of Met 137 from each of the monomersare labeled accordingly. Naringenin completely fills thecoumaroyl-binding and cyclization pockets while the CoA binding tunnelsare highlighted by black arrows. Produced with MOLSCRIPT and renderedwith POV-Ray.

FIG. 4 shows a comparison of chalcone synthase and 3-ketoacyl-CoAthiolase. Ribbon view of the CHS monomer is oriented perpendicular tothe dimer interface. The active site cysteine (Cys 164) and the locationof bound CoA are rendered as ball and stick models. In addition, strandsβ1d and β2d of the cyclization pocket are noted. The reaction catalyzedby CHS is illustrated with the coumaroyl- and malonyl-derived portionsof chalcone, respectively. The thiolase monomer is depicted in the sameorientation as CHS with the Active site cysteine (Cys 125) modeled andthe reaction of thiolase as indicated. Figure prepared with MOLSCRIPTand rendered with POV-Ray.

FIG. 5 collectively shows structures of CHS-Acyl-CoA complexes. Theribbon diagram in panel FIG. 5A (on the top left) is the same as FIG. 3.The CoA binding region depicted in stereo is bounded by a black box inthe upper ribbon diagram. Close-up stereoviews of the C₁₆₄S mutant CoAbinding region for the malonyl- and hexanoyl-CoA complexes are depictedin FIGS. 5B and 5C, respectively. This mutant retains decarboxylationactivity and an acetyl-CoA complex is observed crystallographically forthe malonyl-CoA complex. In each complex, placement of the Met 137 looporiginating from the dyad-related molecule spatially defines one wall ofthe cyclization pocket. Hydrogen bonds are depicted as spheres. Figureprepared with MOLSCRIPT and rendered with POV-Ray.

FIG. 6A shows the CHS-naringenin complex viewed down the CoA-bindingtunnel. The ribbon diagram at the top left has been rotated 90 degreesaround the y-axis from the orientation shown in FIG. 3. This viewapproximates the global orientation of the CHS dimer used for theclose-up view of the naringenin binding site depicted in stereo. Again,the black box highlights the region of CHS shown in stereo close-up.Hydrogen bonds are depicted as dashed cylinders. FIG. 6B illustrates acomparison of the CHS apoenzyme, CHS-naringenin, and CHS-resveratrolstructures. Protein backbone atoms for the three refined structures(apoenzyme, naringenin, and resveratrol) were superimposed by leastsquares fit in O. The position of bound naringenin and resveratrol areshown. For reference, a modeled low energy conformation of chalcone isindicated by dashed cylinders. Strands β1d and β2d for each complex arealso depicted (see FIG. 4). β2d does not change in all the complexesexamined, but β1d moves in the CHS-resveratrol complex. FIG. 6C presentsrepresentative sequence alignment of the β1d-β2d region is given withpositions 255, 266 and 268 highlighted. The first three sequences (SEQID NOS 2-4. respectively in order of appearance) follow a CHS-likecyclization pathway, while the last three (SEQ ID NOS 5-7, respectivelyin order of appearance) use the STS-cyclization pathway. FIG. preparedwith MOLSCRIPT and rendered with POV-Ray.

FIG. 7 presents the proposed reaction mechanism for chalcone synthesis.The three boxed regions labeled 1, 2, and 3 depict the addition ofacetate units derived from malonyl-CoA during the elongation ofpolyketide intermediates. Box 1 is depicted in expanded fashion toillustrate the mechanistic details governing the decarboxylation,enolization, and condensation phase of ketide elongation. Smaller blackarrows depict the flow of electrons. Each acetate unit of themalonyl-CoA thioesters is coded to emphasize the portions of chalconederived from each of three elongation reactions using malonyl-CoA.Cyclization and aromatization of the enzyme bound tetraketide leads toformation of chalcone. Hydrogen bonds are shown as dashed lines.Coenzyme A is symbolized as a circle.

FIG. 8 presents a comparison of the active site volumes of CHS fromalfalfa and CHS from Gerbera hybrida. The active site volumes availablefor binding ketide intermediates were calculated with VOID00 for theCHS-COA complex and for a homology model of GCHS2 with CoA. The cavitiesare shown as a wire mesh. The homology model of GCHS2 was generatedusing MODELER and the volume calculated and displayed as for CHS. Thenumbering scheme is for alfalfa CHS homodimer. Figure prepared withMOLSCRIPT and rendered with POV-Ray.

FIG. 9 shows an example of a computer system in block diagram form.

FIG. 10 shows the chalcone synthase reaction sequence includinginitiation, elongation and cyclization.

FIG. 11 shows an amino acid sequence alignment of P. sylvestris STS (SEQID NO: 8) and M. sativa CHS (SEQ ID NO: 10) along with an evolutionaryintermediate, P. sylvestris CHS (SEQ ID NO: 9).

FIG. 12 shows phenylpropanoid metabolism. From a common linearphenylpropanoid tetraketide intermediate, resveratrol is formed by STSand chalcone is formed by CHS.

FIG. 13 shows different reaction schemes of CHS and STS. STS formsresveratrol via an intramolecular aldol condensation and CHS utilizes anintramolecular Claisen condensation to produce chalcone.

FIG. 14 shows an autoradiographic gel following thin layerchromatography. Wild type CHS produces chalcone, which spontaneouslyconverts to naringenin, the position of which is indicated by the arrowon the left. Wild type STS produces resveratrol, the position of whichis indicated by the arrow of the right. Function conversion of CHS toSTS (i.e., the production of the alternate product from the sameintermediate) results in diminished production of naringenin andincreased production of resveratrol. Various mutants of CHS producevarying degrees of resveratrol, showing that CHS activity can be alteredto STS-like activity to different extents by different mutations.

FIG. 15 shows the crystalline structure of CHS. Circled areas A1 to A4represent regions in which mutations result in the conversion of CHSactivity to STS-like activity. The 18×CHS mutant contains mutations inthese regions.

FIG. 16 shows the crystalline structure of CHS with area B1, mutated inthe 22×CHS mutant circled.

FIG. 17 shows amino acid sequences of homologous sequences from STSfamily members (SEQ ID NOS 11-50, respectively in order of appearancefrom left to right).

FIG. 18 shows the kinetics of the 18xCHS in comparison to the wild typeCHS and STS.

FIG. 19 (SEQ ID NOS 51-57, respectively in order of appearance on theleft, and SEQ ID NOS 58-64, respectively in order of appearance on theright) shows a comparison of the crystal structures of the wild type CHS(alfalfa), two types of STS (pine and peanut) and the 18×CHS mutant.Areas A1 to A4 are as indicated in FIG. 14. A comparison of the aminoacid sequence in these areas is also provided. The stars indicated theresidues mutated in the 8×CHS mutant.

FIG. 20 (SEQ ID NOS 51-57, respectively in order of appearance on theleft, and SEQ ID NOS 58-64, respectively in order of appearance on theright), shows that the 8×CHS mutant has activity that is similar to the18×CHS mutant, i.e. an alteration of the CHS activity to an STS-likeactivity. The 8×CHS mutant contains five mutations in Area A2 and threeadditional changes in Areas A1 and A3. The mutations in the 8×CHS are asubset of the mutations in the 18×CHS mutant, eliminating 10 neutralmutations found in the 18CHS mutant.

FIG. 21 shows the proposed mechanism of cyclization specificity in STSas compared to CHS, which results in the different end-products. STSelimination of terminal CO₂ favors intramolecular C2 to C7 AldolCondensation, while CHS causes intramolecular C6 to C1 ClaisenCondensation coupled to thioester cleavage.

FIG. 22 shows the aldol cyclization switch region as viewed from theCoA-ginding tunnel, involved in the mechanisms depicted in FIG. 21.

DETAILED DESCRIPTION OF THE INVENTION

The phenylpropanoid synthetic pathway in plants produces a class ofcompounds know as anthocyanins, which are used for a variety ofapplications. Anthocyanins are involved in pigmentation and protectionagainst UV photodamage, synthesis of anti-microbial phytoalexins, andare flavonoid inducers of Rhizobium modulation genes 1-4. As medicinalnatural products, the phenylpropanoids exhibit cancer chemopreventiveactivity, as well as anti-mitotic, estrogenic, anti-malarial,anti-oxidant, and antiasthmatic activities. The benefits of consumingred wine, which contains significant amounts of3,4′,5-trihydroxystilbene (resveratrol) and other phenylpropanoids,highlight the dietary importance of these compounds.

Polyketides are a large class of compounds and include a broad range ofantibiotics, immunosuppressants and anticancer agents which togetheraccount for sales of over $5 billion per year. Polyketides are moleculeswhich are an extremely rich source of bioactivities, includingantibiotics (e.g., tetracyclines and erythromycin), anti-cancer agents(e.g., daunomycin), immunosuppressants (e.g., FK506 and rapamycin), andveterinary products (e.g., monensin) and the like. Many polyketides(produced by polyketide synthases) are valuable as therapeutic agents.Polyketide synthases are multifunctional enzymes that catalyze thebiosynthesis of a huge variety of carbon chains differing in length andpatterns of functionality and cyclization.

Chalcone synthase (CHS), a polyketide synthase, plays an essential rolein the biosynthesis of plant phenylpropanoids. CHS supplies4,2′,4′,6′-tetrahydroxychalcone (chalcone) to downstream enzymes thatsynthesize a diverse set of flavonoid phytoalexins and anthocyaninpigments. Synthesis of chalcone by CHS involves the sequentialcondensation of one p-coumaroyl- and three malonyl-Coenzyme-A (CoA)molecules (Kreuzaler and Hahlbrock, Eur. J. Biochem. 56:205-213, 1975).After initial capture of the p-coumaroyl moiety, each subsequentcondensation step begins with decarboxylation of malonyl-CoA at the CHSactive site; the resulting acetyl-CoA carbanion then serves as thenucleophile for chain elongation.

Ultimately, these reactions generate a tetraketide intermediate thatcyclizes by a Claisen condensation into a hydroxylated aromatic ringsystem. This mechanism mirrors those of the fatty acid and polyketidesynthases but with significant differences. CHS uses CoA-thioesters forshuttling substrates and intermediate polyketides instead of the acylcarrier proteins used by the fatty acid synthases. Also, unlike theseenzymes, which function as either multichain or multimodular enzymecomplexes catalyzing distinct reactions at different active sites, CHSfunctions as a unimodular polyketide synthase and carries out a seriesof decarboxylation, condensation, cyclization, and aromatizationreactions at a single active site.

A number of plant and bacterial polyketide synthases related to CHS bysequence identity, including stilbene synthase (STS), bibenzyl synthase(BBS), and acridone synthase (ACS), share a common chemical mechanism,but differ from CHS in their substrate specificity and/or in thestereochemistry of the polyketide cyclization reaction. For example, STScondenses one coumaroyl- and three malonyl-CoA molecules, like CHS, butsynthesizes resveratrol through a structurally distinct cyclizationintermediate.

While the cloning of over 400 CHS-related genes, and characterization ofsome of these proteins, provides insight into their biological function,it remains unclear how these enzymes perform multiple decarboxylationand condensation reactions and how they dictate the stereochemistry ofthe final polyketide cyclization reaction. Furthermore, despitesignificant advances in the biosynthetic manipulation of structurallycomplex and biologically important natural products, there remains alack of structural information on polyketide synthases from any source.

As used herein, “naturally occurring amino acid” and “naturallyoccurring R-group” includes L-isomers of the twenty amino acidsnaturally occurring in proteins. Naturally occurring amino acids areglycine, alanine, valine, leucine, isoleucine, serine, methionine,threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline,histidine, aspartic acid, asparagine, glutamic acid, glutamine,arginine, and lysine. Unless specially indicated, all amino acidsreferred to in this application are in the L-form.

“Unnatural amino acid” and “unnatural R-group” includes amino acids thatare not naturally found in proteins. Examples of unnatural amino acidsincluded herein are racemic mixtures of selenocysteine andselenomethionine. In addition, unnatural amino acids include the D or Lforms of, for example, nor-leucine, para-nitrophenylalanine,homophenylalanine, para-fluorophenylalanine, 3-amino-2-benzylpropionicacid, homoarginines, D-phenylalanine, and the like.

“R-group” refers to the substituent attached to the α-carbon of an aminoacid residue. An R-group is an important determinant of the overallchemical character of an amino acid. There are twenty natural R-groupsfound in proteins, which make up the twenty naturally occurring aminoacids.

“α-carbon” refers to the chiral carbon atom found in an amino acidresidue. Typically, four substituents will be covalently bound to saidα-carbon including an amine group, a carboxylic acid group, a hydrogenatom, and an R-group. The α-carbon atoms can also be referred to bytheir crystal structure coordinates as a convenient reference point.Table 1 provides the structural coordinates of α-carbons found in theactive site of a polyketide of the present invention.

TABLE 1 Amino Acid Active Site-Carbon (SEQ ID Number X Position YPosition Z Position NO: 1) 1 25.378 49.320 57.979 Thr 132 2 26.08945.704 56.981 Ser 133 3 35.423 42.296 66.622 Met 137* 4 25.212 49.97762.196 Gln 161 5 22.745 44.120 51.193 Thr 194 6 19.022 42.892 54.600 Thr197 7 13.850 48.144 50.791 Gly 211 8 22.118 48.048 46.357 Gly 216 913.001 54.666 59.688 Ile 254 10 16.434 48.819 61.334 Gly 256 11 18.71543.328 59.526 Leu 263 12 13.943 47.516 57.567 Phe 265 13 9.252 52.71557.456 Leu 267 14 23.141 53.552 52.148 Ser 338 *Met 137 from the secondmonomer

“Positively charged amino acid” and “positively charged R-group”includes any naturally occurring or unnatural amino acid having a sidechain which is positively charged under normal physiological conditions.Examples of positively charged, naturally occurring amino acids includearginine, lysine, histidine, and the like.

“Negatively charged amino acid” and “negatively charged R-group”includes any naturally occurring or unnatural amino acid having a sidechain which is negatively charged under normal physiological conditions.Examples of negatively charged, naturally occurring amino acids includeaspartic acid, glutamic acid, and the like.

“Hydrophobic amino acid” and “hydrophobic R-group” includes anynaturally occurring or unnatural amino acid that is relatively insolublein water. Examples of naturally occurring hydrophobic amino acids arealanine, leucine, isoleucine, valine, proline, phenylalanine,tryptophan, methionine, and the like.

“Hydrophilic amino acid” and “hydrophilic R-group” includes anynaturally occurring or unnatural amino acid that is relatively solublein water. Examples of naturally occurring hydrophilic amino acidsinclude serine, threonine, tyrosine, asparagine, glutamine, cysteine,and the like.

“Mutant” or “mutated synthase” refers to a polyketide synthasepolypeptide containing amino acid residues that have been substituted ormodified with respect to a wild type polyketide synthase (for example,the alfalfa CHS having the crystal structure coordinates of Protein DataBank (PDB) Accession No. 1BI5, SEQ ID NO:69). Examples of mutant ormutated synthase polypeptides include those having PDB Accession Nos.1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), and 1D6H (SEQ ID NO:69) (thecontent of which are incorporated by reference herein in theirentirety). Further examples of mutant or mutated synthase polypeptidesare set forth in a set of crystal structure coordinates in Appendix C,the 18×CHS mutant (SEQ ID NO:67). Access to the foregoing information inthe Protein Data Bank can be found on the World Wide Web atrscb.org/pdb. The Protein Data Bank is operated by the ResearchCollaboratory for Structural Bioinformatics (RCSB).

The R-groups of known isolated polyketide synthases can be readilydetermined by consulting sequence databases well known in the art, suchas, for example, Genbank. Additional R-groups found inside and/oroutside of the active site may or may not be the same. R-groups may be anatural R-group, unnatural R-group, hydrophobic R-group, hydrophilicR-group, positively charged R-group, negatively charged R-group, and thelike. The term “mutant” refers to the configuration of R-groups withinthe active site and/or groups involved in second-tier interactions, forexample those resulting in the alteration of CHS native activity.

“Non-native” or “non-native synthase” refers to synthase proteins thatare not found in nature, whether isolated or not. A non-native synthasemay, for example, be a mutated synthase (see, for example, PDB AccessionNos. 1D6F, 1D6I, 1D6H and Appendix C).

“Native” or “native synthase” or “wild type synthase” refers to synthaseproteins that are produced in nature, e.g., are not mutants (see, forexample, PDB Accession Nos. 1BI5 (CHS), 1EE0 (2-PS)).

“Isolated” refers to a protein or nucleic acid that has been identifiedand separated from its natural environment. Contaminant components ofits natural environment may include enzymes, hormones, and otherproteinaceous or non-proteinaceous solutes. In one embodiment, theisolated molecule, in the case of a protein, will be purified to adegree sufficient to obtain at least 15 residues of N-terminal orinternal amino acid sequence or to homogeneity by SDS-PAGE underreducing or non-reducing conditions using Coomassie blue or silverstain. In the case of a nucleic acid the isolated molecule willpreferably be purified to a degree sufficient to obtain a nucleic acidsequence using standard sequencing methods.

“Degenerate variations thereof” refers to changing a gene sequence usingthe degenerate nature of the genetic code to encode proteins having thesame amino acid sequence yet having a different gene sequence. Forexample, polyketide synthases of the present invention are based onamino acid sequences. Degenerate gene variations thereof can be madeencoding the same protein due to the plasticity of the genetic code, asdescribed herein.

“Expression” refers to transcription of a gene or nucleic acid sequence,stable accumulation of nucleic acid, and the translation of that nucleicacid to a polypeptide sequence. Expression of genes also involvestranscription of the gene to make RNA, processing of RNA into mRNA ineukaryotic systems, and translation of mRNA into proteins. It is notnecessary for the genes to integrate into the genome of a cell in orderto achieve expression. This definition in no way limits expression to aparticular system or to being confined to cells or a particular celltype and is meant to include cellular, transient, in vitro, in vivo, andviral expression systems in both prokaryotic, eukaryotic cells, and thelike.

“Foreign” or “heterologous” genes refers to a gene encoding a proteinwhose exact amino acid sequence is not normally found in the host cell.

“Promoter” and “promoter regulatory element”, and the like, refers to anucleotide sequence element within a nucleic acid fragment or gene thatcontrols the expression of that gene. These can also include expressioncontrol sequences. Promoter regulatory elements, and the like, from avariety of sources can be used efficiently to promote gene expression.Promoter regulatory elements are meant to include constitutive,tissue-specific, developmental-specific, inducible, subgenomicpromoters, and the like. Promoter regulatory elements may also includecertain enhancer elements or silencing elements that improve or regulatetranscriptional efficiency. Promoter regulatory elements are recognizedby RNA polymerases, promote the binding thereof, and facilitate RNAtranscription.

A polypeptide is a chain of amino acids, regardless of length orpost-translational modification (e.g., glycosylation orphosphorylation). A polypeptide or protein refers to a polymer in whichthe monomers are amino acid residues, which are joined together throughamide bonds. When the amino acids are alpha-amino acids, either theL-optical isomer or the D-optical isomer can be used, the L-isomersbeing typical. A synthase polypeptide of the invention is intended toencompass an amino acid sequence as set forth in SEQ ID NO:1 (see Table2), or SEQ ID NO:1 having one or more mutations. Mutations includedeletions and additions of amino acid residues, and substitutions of oneamino acid residue for another. For example substitutions include: D96A(where D at position 96 of a wild type CHS is changed to A), V98L, V99A,V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F,C164A, Q165H, D255G, H257K, L258V, H266Q, L268K, K269G, D270A, G273D,H303Q, N336A, mutants, variants and conservative substitutions thereofcomprising L- or D-amino acids and include modified sequences such asglycoproteins.

TABLE 2 (SEQ ID NO:1) MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFYFKITNSEHKT ELKEKFQRMC DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVVEVPRLGKEAA VKAIKEWGQP KSKITHLIVC TTSGVDMPGA DYQLTKLLGL RPYVKRYMMYQQGCFAGGTV LRLAKDLAEN NKGARVLVVC SEVTAVTFRG PSDTHLDSLV GQALFGDGAAALIVGSDPVP EIEKPIFEMV WTAQTIAPDS EGAIDGHLRE AGLTFHLLKD VPGIVSKNITKALVEAFEPL GISDYNSIFW IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSACVLFILDEMR KKSTQNGLKT TGEGLEWGVL FGFGPGLTIE TVVLRSVAI

Accordingly, the polypeptides of the invention are intended to covernaturally occurring proteins, as well as those which are recombinantlyor synthetically synthesized. Polypeptide or protein fragments are alsoencompassed by the invention. Fragments can have the same orsubstantially the same amino acid sequence as the naturally occurringprotein. A polypeptide or peptide having substantially the same sequencemeans that an amino acid sequence is largely, but not entirely, thesame, but retains a functional activity of the sequence to which it isrelated. In general polypeptides of the invention include peptides, orfull-length protein, that contains substitutions, deletions, orinsertions into the protein backbone, that would still have anapproximately 70%-90% homology to the original protein over thecorresponding portion. A yet greater degree of departure from homologyis allowed if like-amino acids, i.e. conservative amino acidsubstitutions, do not count as a change in the sequence.

A polypeptide may be substantially related but for a conservativevariation, such polypeptides being encompassed by the invention. Aconservative variation denotes the replacement of an amino acid residueby another, biologically similar residue. Examples of conservativevariations include the substitution of one hydrophobic residue such asisoleucine, valine, leucine or methionine for another, or thesubstitution of one polar residue for another, such as the substitutionof arginine for lysine, glutamic for aspartic acids, or glutamine forasparagine, and the like. Other illustrative examples of conservativesubstitutions include the changes of: alanine to serine; arginine tolysine; asparagine to glutamine or histidine; aspartate to glutamate;cysteine to serine; glutamine to asparagine; glutamate to aspartate;glycine to proline; histidine to asparagine or glutamine; isoleucine toleucine or valine; leucine to valine or isoleucine; lysine to arginine,glutamine, or glutamate; methionine to leucine or isoleucine;phenylalanine to tyrosine, leucine or methionine; serine to threonine;threonine to serine; tryptophan to tyrosine; tyrosine to tryptophan orphenylalanine; valine to isoleucine or leucine, and the like. The term“conservative variation” also includes the use of a substituted aminoacid in place of an unsubstituted parent amino acid provided thatantibodies raised to the substituted polypeptide also immunoreact withthe unsubstituted polypeptide.

Modifications and substitutions are not limited to replacement of aminoacids. For a variety of purposes, such as increased stability,solubility, or configuration concerns, one skilled in the art willrecognize the need to introduce, (by deletion, replacement, or addition)other modifications. Examples of such other modifications includeincorporation of rare amino acids, dextra-amino acids, glycosylationsites, cytosine for specific disulfide bridge formation. The modifiedpeptides can be chemically synthesized, or the isolated gene can besite-directed mutagenized, or a synthetic gene can be synthesized andexpressed in bacteria, yeast, baculovirus, tissue culture and so on.

Chalcone synthase polypeptides of the invention include synthasepolypeptides from plants, prokaryotes, eukaryotes, including, forexample, invertebrates, mammals and humans and include sequences as setforth in SEQ ID NO:1, as well as sequences that have at least 50%homology, preferably at least 60% homology, more preferably at least 70%homology to the sequence of SEQ ID NO:1, fragments, variants, orconservative substitutions of any of the foregoing sequences.

The term “variant” refers to polypeptides modified at one or more aminoacid residues yet still retain the biological activity of a synthasepolypeptide. Variants can be produced by any number of means known inthe art, including, for example, methods such as, for example,error-prone PCR, shuffling, oligonucleotide-directed mutagenesis,assembly PCR, sexual PCR mutagenesis, and the like, as well as anycombination thereof.

By “substantially identical” is meant a polypeptide or nucleic acidexhibiting at least 50%, preferably 85%, more preferably 90%, and mostpreferably 95% homology to a reference amino acid or nucleic acidsequence.

Sequence homology and identity are often measured using sequenceanalysis software (e.g., Sequence Analysis Software Package of theGenetics Computer Group, University of Wisconsin Biotechnology Center,1710 University Avenue, Madison, Wis. 53705). The term “identity” in thecontext of two or more nucleic acids or polypeptide sequences, refers totwo or more sequences or subsequences that are the same or have aspecified percentage of amino acid residues or nucleotides that are thesame when compared and aligned for maximum correspondence over acomparison window or designated region as measured using any number ofsequence comparison algorithms or by manual alignment and visualinspection. The term “homology” in the context of two or more nucleicacids or polypeptide sequences, refers to two or more sequences orsubsequences that are homologous or have a specified percentage of aminoacid residues or nucleotides that are homologous when compared andaligned for maximum correspondence over a comparison window ordesignated region as measured using any number of sequence comparisonalgorithms or by manual alignment and visual inspection. Programs asmentioned above allow for amino acid substitutions with similar aminoacids matches by assigning degrees of homology to determine a degree ofhomology between the sequences being compared.

For sequence comparison, typically one sequence acts as a referencesequence, to which test sequences are compared. When using a sequencecomparison algorithm, test and reference sequences are entered into acomputer, subsequence coordinates are designated, if necessary, andsequence algorithm program parameters are designated. Default programparameters can be used, or alternative parameters can be designated. Thesequence comparison algorithm then calculates the percent sequenceidentities for the test sequences relative to the reference sequence,based on the program parameters.

A “comparison window”, as used herein, includes reference to a segmentof any one of the number of contiguous positions selected from the groupconsisting of from 20 to 600, usually about 50 to about 200, moreusually about 100 to about 150 in which a sequence may be compared to areference sequence of the same number of contiguous positions after thetwo sequences are optimally aligned. Methods of alignment of sequencefor comparison are well-known in the art. Optimal alignment of sequencesfor comparison can be conducted, e.g., by the local homology algorithmof Smith & Waterman, Adv. Appl. Math. 2:482, 1981, by the homologyalignment algorithm of Needleman & Wunsch, J. Mol. Biol 48:443, 1970, bythe search for similarity method of Person & Lipman, Proc. Nat'l. Acad.Sci. USA 85:2444, 1988, by computerized implementations of thesealgorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin GeneticsSoftware Package, Genetics Computer Group, 575 Science Dr., Madison,Wis.), or by manual alignment and visual inspection. Other algorithmsfor determining homology or identity include, for example, in additionto a BLAST program (Basic Local Alignment Search Tool at the NationalCenter for Biological Information), ALIGN, AMAS (Analysis of MultiplyAligned Sequences), AMPS (Protein Multiple Sequence Alignment), ASSET(Aligned Segment Statistical Evaluation Tool), BANDS, BESTSCOR, BIOSCAN(Biological Sequence Comparative Analysis Node), BLIMPS (BLocks IMProvedSearcher), FASTA, Intervals & Points, BMB, CLUSTAL V, CLUSTAL W,CONSENSUS, LCONSENSUS, WCONSENSUS, Smith-Waterman algorithm, DARWIN, LasVegas algorithm, FNAT (Forced Nucleotide Alignment Tool), Framealign,Framesearch, DYNAMIC, FILTER, FSAP (Fnstensky Sequence AnalysisPackage), GAP (Global Alignment Program), GENAL, GIBBS, GenQuest, ISSC(Sensitive Sequence Comparison), LALIGN (Local Sequence Alignment), LCP(Local Content Program), MACAW (Multiple Alignment Construction &Analysis Workbench), MAP (Multiple Alignment Program), MBLKP, MBLKN,PIMA (Pattern-Induced Multi-sequence Alignment), SAGA (SequenceAlignment by Genetic Algorithm) and WHAT-IF. Such alignment programs canalso be used to screen genome databases to identify polynucleotidesequences having substantially identical sequences. A number of genomedatabases are available, for example, a substantial portion of the humangenome is available as part of the Human Genome Sequencing Project (J.Roach, on the World Wide Web atweber.u.Washington.edu/˜roach/human_genome_progress2.html) (Gibbs,1995). At least twenty-one other genomes have already been sequenced,including, for example, M. genitalium (Fraser et al., 1995), M.jannaschii (Bult et al., 1996), H. influenzae (Fleischmann et al.,1995), E. coli (Blattner et al., 1997), and yeast (S. cerevisiae) (Meweset al., 1997), and D. melanogaster (Adams et al., 2000). Significantprogress has also been made in sequencing the genomes of model organism,such as mouse, C. elegans, and Arabadopsis sp. Several databasescontaining genomic information annotated with some functionalinformation are maintained by different organization, and are accessiblevia the internet, for example, on the World Wide Web at tigr.org/tdb,genetics.wisc.edu, genome-www.stanford.edu, hiv-web.lanl.gov,ncbi.nlm.nih.gov, cbi.ac.uk, Pasteur.fr/other/biology, andgenome.wi.mlt.edu.

One example of a useful algorithm is BLAST and BLAST 2.0algorithms,which are described in Altschul et al., Nuc. Acids Res. 25:33 89-3402,1977, and Altschul et al., J. Mol. Biol. 215:403-410, 1990,respectively. Software for performing BLAST analyses is publiclyavailable through the National Center for Biotechnology Informationavailable on the World Wide Web at ncbi.nlm.nih.gov). This algorithminvolves first identifying high scoring sequence pairs (HSPs) byidentifying short words of length W in the query sequence, which eithermatch or satisfy some positive-valued threshold score T when alignedwith a word of the same length in a database sequence. T is referred toas the neighborhood word score threshold (Altschul et al., supra). Theseinitial neighborhood word hits act as seeds for initiating searches tofind longer HSPs containing them. The word hits are extended in bothdirections along each sequence for as far as the cumulative alignmentscore can be increased. Cumulative scores are calculated using, fornucleotide sequences, the parameters M (reward score for a pair ofmatching residues; always >0). For amino acid sequences, a scoringmatrix is used to calculate the cumulative score. Extension of the wordhits in each direction are halted when: the cumulative alignment scorefalls off by the quantity X from its maximum achieved value; thecumulative score goes to zero or below, due to the accumulation of oneor more negative-scoring residue alignments; or the end of eithersequence is reached. The BLAST algorithm parameters W, T, and Xdetermine the sensitivity and speed of the alignment. The BLASTN program(for nucleotide sequences) uses as defaults a wordlength (W) of 11, anexpectation (E) of 10, M=5, N=−4 and a comparison of both strands. Foramino acid sequences, the BLASTP program uses as defaults a wordlengthof 3, and expectations (E) of 10, and the BLOSUM62 scoring matrix (seeHenikoff& Henikoff, Proc. Natl. Acad. Sci. USA 89:10915, 1989)alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparisonof both strands.

The BLAST algorithm also performs a statistical analysis of thesimilarity between two sequences (see, e.g., Karlin & Altschul, Proc.Natl. Acad. Sci. USA 90:5873, 1993). One measure of similarity providedby BLAST algorithm is the smallest sum probability (P(N)), whichprovides an indication of the probability by which a match between twonucleotide or amino acid sequences would occur by chance. For example, anucleic acid is considered similar to a references sequence if thesmallest sum probability in a comparison of the test nucleic acid to thereference nucleic acid is less than about 0.2, more preferably less thanabout 0.01, and most preferably less than about 0.001.

In one embodiment, protein and nucleic acid sequence homologies areevaluated using the Basic Local Alignment Search Tool (“BLAST”) Inparticular, five specific BLAST programs are used to perform thefollowing task:

-   -   (1) BLASTP and BLAST3 compare an amino acid query sequence        against a protein sequence database;    -   (2) BLASTN compares a nucleotide query sequence against a        nucleotide sequence database;    -   (3) BLASTX compares the six-frame conceptual translation        products of a query nucleotide sequence (both strands) against a        protein sequence database;    -   (4) TBLASTN compares a query protein sequence against a        nucleotide sequence database translated in all six reading        frames (both strands); and    -   (5) TBLASTX compares the six-frame translations of a nucleotide        query sequence against the six-frame translations of a        nucleotide sequence database.

The BLAST programs identify homologous sequences by identifying similarsegments, which are referred to herein as “high-scoring segment pairs,”between a query amino or nucleic acid sequence and a test sequence whichis preferably obtained from a protein or nucleic acid sequence database.High-scoring segment pairs are preferably identified (i.e., aligned) bymeans of a scoring matrix, many of which are known in the art.Preferably, the scoring matrix used is the BLOSUM62 matrix (Gonnetetal., Science 256:1443-1445, 1992; Henikoff and Henikoff, Proteins17:49-61, 1993). Less preferably,the PAM or PAM250 matrices may also beused (see, e.g., Schwartz and Dayhoff, eds., 1978, Matrices forDetecting Distance Relationships. Atlas of Protein Sequence andStructure, Washington: National Biomedical Research Foundation). BLASTprograms are accessible through the U.S. National Library of Medicine,e.g., on the World Wide Web at ncbi.nlm.nih.gov.

The parameters used with the above algorithms may be adapted dependingon the sequence length and degree of homology studied. In someembodiments, the parameters may be the default parameters used by thealgorithms in the absence of instructions from the user.

By a “substantially pure polypeptide” is meant a synthase polypeptide(e.g., a chalcone synthase) which has been separated from componentswhich naturally accompany it. Typically, the polypeptide issubstantially pure when it is at least 60%, by weight, free from theproteins and naturally-occurring organic molecules with which it isnaturally associated. Preferably, the preparation is at least 75%, morepreferably at least 90%, and most preferably at least 99%, by weight,synthase polypeptide. A substantially pure synthase polypeptide may beobtained, for example, by extraction from a natural source; byexpression of a recombinant nucleic acid encoding an synthasepolypeptide; or by chemically synthesizing the protein. Purity can bemeasured by any appropriate method (e.g., column chromatography,polyacrylamide gel electrophoresis, or by HPLC analysis).

One aspect of the invention resides in obtaining crystals of thesynthase polypeptide, chalcone synthase, of sufficient quality todetermine the three dimensional (tertiary) structure of the protein byX-ray diffraction methods. The knowledge obtained concerning thethree-dimensional structure of chalcone synthase can be used in thedetermination of the three dimensional structure of other synthasepolypeptides in the polyketide synthesis pathway. The structuralcoordinates of chalcone synthase can be used to develop new polyketidesynthesis enzymes or synthase inhibitors using various computer models.Based on the structural coordinates of the chalcone synthase polypeptide(e.g., the three dimensional protein structure), as described herein,novel polyketide synthases can be engineered. In addition, smallmolecules which mimic or are capable of interacting with a functionaldomain of a synthase molecule, can be designed and synthesized tomodulate chalcone synthase, pyrone synthase, and other polyketidesynthase biological functions as well as the biological functions ofother polyketide synthases. Accordingly, in one embodiment, theinvention provides a method of “rational” enzyme or drug design. Anotherapproach to “rational” enzyme or drug design is based on a lead compoundthat is discovered using high throughput screens; the lead compound isfurther modified based on a crystal structure of the binding regions ofthe molecule in question. Accordingly, another aspect of the inventionis to provide related protein sequences or material which is a startingmaterial in the rational design of new synthases or drugs which lead tothe synthesis of new polyketides or modify the polyketide synthesispathway.

“Active Site” refers to a site in a synthase defined by amino acidresidues that interact with substrate and facilitate a biosyntheticreaction that allows one or more products to be produced. For example,an active site is comprised of α-carbon atoms that are indirectly linkedvia peptide bonds and have the structural coordinates disclosed in Table1±2.3 angstroms. Other active site amino acids for chalcone synthaseinclude C164, H303, and N336. The position in three-dimensional space ofan α-carbon at the active site of a synthase and of R-groups associatedtherewith can be determined using techniques such as three-dimensionalmodeling, X-ray crystallography, and/or techniques associated therewith.Active sites can be specified by a set of amino acid residues. Otherresidues can play a reole in substrate specificity and enzyme activityby modulating size, shape, charge, and the like of the active site. Inaddition, second tier residues may also modulate the specificity and/oractivity of the enzyme.

In CHS, at least five areas of primary sequence containing residues thatplay a role modulating enzyme specificity and/or activity are found.Each area contains a total of about four to about fifteen amino acidresidues. Within each area, about three to six, and preferably four orfive amino acid residues that interact with substrate are found.Residues may be directly within or lining the active site to modulatespecificity and/or activity. Residues may also be involved in secondtier interactions that modulate the specificity and/or activity of theactive site, without being physically located within the active site.Various mutants of these residues have been prepared to evaluate therole of these residues in CHS function and activity, including substratespecificity and product formation. Table 3 presents some of themutations of CHS that have been made to affect CHS function.

TABLE 3 Mutants of CHS Mutant Mutant Name Code Mutations relative toalfalfa CHS A4 0002 A4 (L268K, K269G, D270A, G273D) 14B 1200 A1 (V98L,)(=6xCHS) A2 (T131S, S133T, G134T, V135P, M137L) 2B 2200 A1 (D96A, V98L,V99A, V100M) A2 (T131S, S133T, G134T, V135P, M137L) 16B 1210 A1 (V98L,)(=8xCHS) A2 (T131S, S133T, G134T, V135P, M137L) A3 (M158G, Y160F) 4B2211 A1 (D96A, V98L, V99A, V100M) A2 (T131S, S133T, G134T, V135P, M137L)A3 (M158G, Y160F) A4 (K269G) 6B 1220 A1 (V98L,) A2 (T131S, S133T, G134T,V135P, M137L) A3 (Y157V, M158G, M159V, Y160F, Q165H); 18xCHS 2222 A1(D96A, V98L, V99A, V100M) A2 (T131S, S133T, G134T, V135P, M137L) A3(Y157V, M158G, M159V, Y160F, Q165H) A4 (L268K, K269G, D270A, G273D)22xCHS 2222 + A1 (D96A, V98L, V99A, V100M) Area B1 A2 (T131S, S133T,G134T, V135P, M137L) A3 (Y157V, M158G, M159V, Y160F, Q165H) B1 (D255G,H257K, L258V, H266Q) A4 (L268K, K269G, D270A, G273D)

A polyketide synthase can be divided into regional areas A1-A4 and B1.Areas A1 and A3 flank area A2, from below and above, respectively (seeFIG. 15). Both areas seem to have importance mainly in regards tocompensatory steric changes which allow a proline induced kink in areaA2 relative to the CHS position. The backbone C-alpha traces of A1 andA3 do not actually vary much from CHS to STS, but length of indicatedresidues does. In area A1, amino acids involved in the modulation ofenzyme specificity and/or activity for chalcone synthase include D96,V98, V99 and V100. In area A3, such amino acids include Y157, M158,M159, Y160 and Q165. Mutations at V98 and V99 in area A1, and at M158and Y160 in area A3 appear especially important for modifying activity.

Area A2 appears to be the most important area, and is located at thedimer interface, directly between the active site cavities of eachmonomer. In area A2 amino acids involved in the modulation of enzymespecificity and/or activity include T131, S133, G134, V135 and M137.Mutations at G134 and V135 appear especially important for modifyingactivity.

Area A4 is located on the outside of the protein, near the active siteentrance. A4 mutations made to wild type CHS seems to have no effect oncyclization specificity, indicating that this area is not important tothe conversion of activity seen in the certain mutants, for example, the18xCHS mutant. However, this area may be important in the improvementsto conversion seen with the addition of four more mutants (at B1, seeFIG. 16 and below) in the 22× CHS mutant. In area A4, amino acidsinvolved in the modulation of enzyme specificity and/or activity includeL268, K269, D270 and G273.

Area B1 flanks A4 and bridges the gap between A1-A3 and A4. In area B1,amino acids involved in the modulation of enzyme specificity and/oractivity include D255, H257L258 and H266. These mutations are in an areapredicted in by Ferrer, et al. and are important for cyclizationspecificity.

“Altered substrate specificity” or “altered activity” includes a changein the ability of a mutant synthase to use a particular substrate and/orproduce a polyketide product as compared to a non-mutated synthase.Altered substrate specificity may include the ability of a synthase toexhibit different enzymatic parameters relative to a non-mutatedsynthase (K_(m), V_(max), etc), use different substrates, and/or produceproducts that are different from those of known synthases.

“Structure coordinates” refers to Cartesian coordinates (x, y, and zpositions) derived from mathematical equations involving Fouriersynthesis as determined from patterns obtained via diffraction of amonochromatic beam of X-rays by the atoms (scattering centers) of apolyketide synthase molecule in crystal form. Diffraction data are usedto calculate electron density maps of repeating protein units in thecrystal (unit cell). Electron density maps are used to establish thepositions of individual atoms within a crystal's unit cell. The term“crystal structure coordinates” refers to mathematical coordinatesderived from mathematical equations related to the patterns obtained ondiffraction of a monochromatic beam of X-rays by the atoms (scatteringcenters) of a synthase polypeptide (e.g., a chalcone synthase proteinmolecule) in crystal form. The diffraction data are used to calculate anelectron density map of the repeating unit of the crystal. The electrondensity maps are used to establish the positions of the individual atomswithin the unit cell of the crystal. The crystal structure coordinatesof a synthase can be obtained from crystals and can also be obtained bymeans of computational analysis.

The term “selenomethionine substitution” refers to the method ofproducing a chemically modified form of the crystal of a synthase (e.g.,a chalcone synthase). The synthase protein is expressed by bacteria inmedia that is depleted in methionine and supplement withselenomethionine. Selenium is thereby incorporated into the crystal inplace of methionine sulfurs. The location(s) of selenium are determinedby X-ray diffraction analysis of the crystal. This information is usedto generate the phase information used to construct a three-dimensionalstructure of the protein.

“Heavy atom derivatization” refers to a method of producing a chemicallymodified form of a synthase crystal. In practice, a crystal is soaked ina solution containing heavy atom salts or organometallic compounds,e.g., lead chloride, gold thiomalate, thirerosal, uranyl acetate, andthe like, which can diffuse through the crystal and bind to theprotein's surface. Locations of the bound heavy atoms can be determinedby X-ray diffraction analysis of the soaked crystal. This information isthen used to construct phase information which can then be used toconstruct three-dimensional structures of the enzyme as described inBlundel, T. L., and Johnson, N. L., Protein Crystallography, AcademicPress (1976), which is incorporated by reference herein.

“Unit cell” refers to a basic parallelepiped shaped block. Regularassembly of such blocks may construct the entire volume of a crystal.Each unit cell comprises a complete representation of the unit pattern,the repetition of which builds up the crystal.

“Mutagenesis” refers to the changing of one R-group for another asdefined herein. This can be most easily performed by changing the codingsequence of the nucleic acid encoding the amino acid residue. In thecontext of the present invention, mutagenesis does not change the carboncoordinates beyond the limits defined herein.

“Space Group” refers to the arrangement of symmetry elements within acrystal.

“Molecular replacement” refers to generating a preliminary model of apolyketide synthase whose structural coordinates are unknown, byorienting and positioning a molecule whose structural coordinates areknown within the unit cell of the unknown crystal so as best to accountfor the observed diffraction pattern of the unknown crystal. Phases canthen be calculated from this model and combined with the observedamplitudes to give an approximate Fourier synthesis of the structurewhose coordinates are unknown. This in turn can be subject to any of theseveral forms of refinement to provide a final, accurate structure ofthe unknown crystal (Lattman, E., 1985, in Methods in Enzymology, 115.55-77; Rossmann, M G., ed., “The Molecular Replacement Method” 1972,Int, Sci. Rev. Ser., No. 13, Gordon & Breach, New York). Using structurecoordinates of the polyketide synthase provided herein (see e.g., PDBAccession Numbers) molecular replacement may be used to determine thestructural coordinates of a crystalline mutant, homologue, or adifferent crystal form of polyketide synthase.

A “synthase” or a “polyketide synthase” includes any one of a family ofenzymes that catalyze the formation of polyketide compounds. Polyketidesynthases are generally homodimers, with each monomer beingenzymatically acitve.

“Substrate” refers to the Coenzyme-A (CoA) thioesters that are acted onby the polyketide synthases and mutants thereof disclosed herein, suchas malonyl-CoA, coumaroyl-CoA, hexamoyl-CoA, ACP or NAC thioesters andthe like.

The present invention relates to crystallized polyketide synthases andmutants thereof from which the position of specific α-carbon atoms andR-groups associated therewith comprising the active site can bedetermined in three-dimensional space. The invention also relates tostructural coordinates of said polyketide synthases, use of saidstructural coordinates to develop structural information related topolyketide synthase homologues, mutants, and the like, and to crystalforms of such synthases. Furthermore, the invention, as disclosedherein, provides a method whereby said α-carbon structural coordinatesspecifically determined for atoms comprising the active site of saidsynthase, as shown in Table 1 and including C164, H303, and N336, can beused to develop synthases wherein R-groups associated with active siteα-carbon atoms are different from the R-groups found in native CHS,e.g., are mutant synthases. In addition, the present invention providesfor production of mutant polyketide synthases based on the structuralinformation of synthases (and provided herein) and for use of saidmutant synthases to make a variety of polyketide compounds using avariety of substrates (as described in PCT Application US00/20674, filedJul. 27, 2000, incorporated by reference in its entirety herein). Thepresent invention also provides methods of producing novel mutantpolyketide synthases by comparing the crystal structures of twodifferent polyketide synthases.

The present invention further provides, for the first time, crystals ofseveral polyketide synthases, as exemplified by chalcone synthase (CHS;PDB Accession No. 1B15, SEQ ID NO:69), stilbene synthase (STS; Pinussylvestris, pine—Appendix A, SEQ ID NO:65; and Arachis hypogaea,peanut—Appendix B, SEQ ID NO:66), and pyrone synthase (2-PS; PDBAccession No. 1EE0, SEQ ID NO:68). Also provided are coordinates forcrystals which are grown in the presence and absence of substrate,substrate analogues, and products, thus allowing definition of thestructural or atomic coordinates associated therewith. Said structuralcoordinates allow determination of the carbon atoms comprising theactive site, R-groups associated therewith, and the interaction of saidα-carbons and said R-groups with each other. For example, Table 4identifies various substrates and products that were grown with chalconesynthase as well as their PDB accession numbers, all of which areincorporated by reference herein in their entirety.

TABLE 4 Complex PDB Accession No. (SEQ ID NO:) CHS-coA complex 1BQ6 (SEQID NO: 69) CHS-malonyl-CoA complex 1CML (SEQ ID NO: 69) CHS-hexanoyl-CoAcomplex 1CHW (SEQ ID NO: 69) CHS-naringenin complex 1CGK (SEQ ID NO: 69)CHS-resveratrol complex 1CGZ (SEQ ID NO: 69)

The crystals of the present invention belong to the tetragonal spacegroup. The unit cell dimensions vary by a few angstroms between crystalsbut on average belong to the space groups with unit cell dimensions asin Table 5.

TABLE 5 Crystals of Polyketide Synthases Space Unit Cell DimensionsCrystal Group a (Å) b (Å) c (Å) α (°) β (°) γ (°) CHS P 32 2 1 97.5497.54 65.52 90.00 90.00 120.00 (alfalfa) (SEQ ID NO: 1) STS P2 (1)57.221 361.291 57.317 90.00 98.39 90.00 (pine) (SEQ ID NO: 65) STS P2(1) 74.348 101.747 113.609 90.00 108.84 90.00 (peanut) (SEQ ID NO: 66)2-PS P 31 2 1 83.41 83.41 240.62 90.00 90.00 120.00 (SEQ ID NO: 68)18xCHS P2 (1) 71.638 59.753 82.539 90.00 108.166 90.00 (SEQ ID NO: 67)

Crystal structures are preferably obtained at a resolution of about 1.56angstroms to about 3 angstroms for a polyketide synthase in the presenceand in the absence of bound substrate or substrate analog. Coordinatesfor a polyketide synthase in the absence of a substrate bound in theactive site have been deposited at the Protein Data Bank, accessionnumber 1BI5. Those skilled in the art understand that a set of structurecoordinates determined by X-ray crystallography is not without standarderror. Therefore, for the purpose of this invention, any set ofstructure coordinates wherein the active site α-carbons of a polyketidesynthase, synthase homologue, or mutants thereof, have a root meansquare deviation less than ±2.3 angstroms when superimposed using thestructural coordinates listed in Table 1 and PDB Accession No. 1BI5,shall be considered identical.

A schematic representation of the three-dimensional shape of a CHShomodimer is shown in FIG. 2 a, which was prepared by MOLSCRIPT(Kraulis, J. Appl. Crystallogr. 24:946-950, 1991). CHS functions as ahomodimer of two 42 kDa polypeptides. The structure of CHS reveals thatthe enzyme forms a symmetric dimer with each monomer related by a 2-foldcrystallographic axis. The dimer interface buries approximately 1580angstroms with interactions occurring along a fairly flat surface. Twodistinct structural features delineate the ends of this interface.First, the N-terminal helix of monomer A entwines with the correspondinghelix of monomer B. Second, a tight loop containing a cis-peptide bondbetween Met₁₃₇ and Pro₁₃₈ exposes the methionine sidechain as a knob onthe monomer surface. Across the interface, Met₁₃₇ protrudes into a holefound in the surface of the adjoining monomer to form part of thecyclization pocket (discussed below).

The CHS homodimer contains two functionally independent active sites(Tropf, et al, J. Biol. Chem. 270:7922-7928, 1995). Consistent with thisinformation, bound CoA thioesters and product analogs occupy both activesites of the homodimer in the CHS complex structures. These structuresidentify the location of the active site at the cleft between the upperand lower domains of each monomer. Each active site consists almostentirely of residues from a single monomer, with Met₁₃₇ from theadjoining monomer being the only exception. A detailed description ofthe active site structure is presented in the Examples section, below.

An isolated, polyketide synthase of the invention comprises at leastfourteen active site α-carbons having the structural coordinates ofTable 1±2.3 angstroms. The active site α-carbons of Table 1 generallyare not all contiguous, i.e., are not adjacent to one another in theprimary amino acid sequence of a polyketide synthase due to interveningamino acid residues between various active site α-carbons. Nevertheless,it should be appreciated that certain active site α-carbons can beadjacent to one another in some instances. Active site α-carbons arenumbered in Table 1 for convenience only and may be situated in anysuitable order in the primary amino acid sequence that achieves thestructural coordinates given in Table 1.

An appropriate combination of R-groups, linked to active site α-carbons,can facilitate the formation of one or more desired reaction products.The combination of R-groups selected for use in a synthase can be anycombination other than the ordered arrangements of R-groups found inknown native isolated polyketide synthases. Typically, R-groups found onactive site α-carbons are those found in naturally occurring aminoacids. In some embodiments, however, R-groups other than those found innaturally occurring amino acids can be used.

The present invention permits the use of molecular design techniques todesign, select, and synthesize mutant polyketide synthases that producedifferent and/or novel polyketide compounds using the same substrates.Mutant proteins of the present invention and nucleic acids encoding thesame can be designed by genetic manipulation based on structuralinformation about polyketide synthases. For example, one or moreR-groups associated with the active site α-carbon atoms of CHS can bechanged by altering the nucleotide sequence of the corresponding CHSgene, thus making one or more mutant polyketide synthases. Such geneticmanipulations can be guided by structural information concerning theR-groups found in the active site α-carbons when substrate is bound tothe protein upon crystallization. Alternatively, mutant polyketidesyntases can be prepared by standard protocols for polypeptide synthesisas is well known in the art.

Mutant proteins of the present invention may be prepared in a number ofways available to the skilled artisan. For example, the gene encodingwild-type CHS may be mutated at those sites identified herein ascorresponding to amino acid residues identified in the active site bymeans currently available to the artisan skilled in molecular biologytechniques. Said techniques include oligonucleotide-directedmutagenesis, deletion, chemical mutagenesis, and the like. The proteinencoded by the mutant gene is then produced by expressing the gene in,for example, a bacterial or plant expression system.

Alternatively, polyketide synthase mutants may be generated by sitespecific-replacement of a particular amino acid with an unnaturallyoccurring amino acid. As such, polyketide synthase mutants may begenerated through replacement of an amino acid residue or a particularcysteine or methionine residue with selenocysteine or selenomethionine.This may be achieved by growing a host organism capable of expressingeither the wild-type or mutant polypeptide on a growth medium depletedof natural cysteine or methionine or both and growing on medium enrichedwith either selenocysteine, selenomethionine, or both. These and similartechniques are described in Sambrook et al., (Molecular Cloning, ALaboratory Manual, 2^(nd) Ed. (1989) Cold Spring Harbor LaboratoryPress).

Another suitable method of creating mutant synthases of the presentinvention is based on a procedure described in Noel and Tsal (1989) J.Cell. Biochem., 40:309-320. In so doing, the nucleic acids encoding saidpolyketide synthase can be synthetically produced using oligonucleotideshaving overlapping regions, said oligonucleotides being degenerate atspecific bases so that mutations are induced. Alternatively, traditionalmethod of protein or polypeptide synthesis may be used.

According to the present invention, nucleic acid sequences encoding amutated polyketide synthase can be produced by the methods describedherein, or any alternative methods available to the skilled artisan. Indesigning the nucleic acid sequence of interest, it may be desirable toreengineer said gene for improved expression in a particular expressionsystem. For example, it has been shown that many bacterially derivedgenes do not express well in plant systems. In some cases, plant-derivedgenes do not express well in bacteria. This phenomenon may be due to thenon-optimal G+C content and/or A+T content of said gene relative to theexpression system being used. For example, the very low G+C content ofmany bacterial genes results in the generation of sequences minicking orduplicating plant gene control sequences, that are highly A+T rich. Thepresence of A+T rich sequences within the genes introduced into plants(e.g., TATA box regions normally found in promoters) may result inaberrant transcription of the gene(s). In addition, the presence ofother regulatory sequences residing in the transcribed mRNA (e.g.polyadenylation signal sequences (AAUAAA) or sequences complementary tosmall nuclear RNAs involved in pre-mRNA splicing) may lead to RNAinstability. Therefore, one goal in the design of genes is to generatenucleic acid sequences that have a G+C content that affords mRNAstability and translation accuracy for a particular expression system.

Due to the plasticity afforded by the redundancy of the genetic code(i.e., many amino acids are specified by more than one codon), evolutionof the genomes of different organisms or classes of organisms hasresulted in differential usage of redundant codons. This “codon bias” isreflected in the mean base composition of protein coding regions. Forexample, organisms with relatively low G+C contents utilize codonshaving A or T in the third position of redundant codons, whereas thosehaving higher G+C contents utilize codons having G or C in the thirdposition. Therefore, in reengineering genes for expression, one may wishto determine the codon bias of the organism in which the gene is to beexpressed. Looking at the usage of the codons as determined for genes ofa particular organism deposited in GenBank can provide this information.After determining the bias thereof, the new gene sequence can beanalyzed for restriction enzyme sites as well as other sites that couldaffect transcription such as exon:intron junctions, polyA additionsignals, or RNA polymerase termination signals.

Genes encoding polyketide synthases can be placed in an appropriatevector, depending on the artisan's interest, and can be expressed usinga suitable expression system. An expression vector, as is well known inthe art, typically includes elements that permit replication of saidvector within the host cell and may contain one or more phenotypicmarkers for selection of cells containing said gene. The expressionvector will typically contain sequences that control expression such aspromoter sequences, ribosome binding sites, and translational initiationand termination sequences. Expression vectors may also contain elementssuch as subgenomic promoters, a repressor gene or various activatorgenes. The artisan may also choose to include nucleic acid sequencesthat result in secretion of the gene product, movement of said productto a particular organelle such as a plant plastid (see U.S. Pat. Nos.4,762,785; 5,451,513 and 5,545,817, which are incorporated by referenceherein) or other sequences that increase the ease of peptidepurification, such as an affinity tag.

A wide variety of expression control sequences are useful in expressingthe mutated polyketide synthases when operably linked thereto. Suchexpression control sequences include, for example, the early and latepromoters of SV40 for animal cells, the lac system, the trp system,major operator and promoter systems of phage S, and the control regionsof coat proteins, particularly those from RNA viruses in plants. In E.coli, a useful transcriptional control sequence is the T7 RNA polymerasebinding promoter, which can be incorporated into a pET vector asdescribed by Studier et al., (1990) Methods Enzymology, 185:60-89, whichis incorporated by reference herein.

For expression, a desired gene should be operably linked to theexpression control sequence and maintain the appropriate reading frameto permit production of the desired polyketide synthase. Any of a widevariety of well-known expression vectors are of use to the presentinvention. These include, for example, vectors comprising segments ofchromosomal, non-chromosomal and synthetic DNA sequences such as thosederived from SV40, bacterial plasmids including those from E. coli suchas col E1, pCR1, pBR322 and derivatives thereof, pMB9), wider host rangeplasmids such as RP4, phage DNA such as phage S, NM989, M13, and othersuch systems as described by Sambrook et al., (Molecular Cloning, ALaboratory Manual, 2^(nd) Ed. (1989) Cold Spring Harbor LaboratoryPress), which is incorporated by reference herein.

A wide variety of host cells are available for expressing synthasemutants of the present invention. Such host cells include, for example,bacteria such as E. coli, Bacillus and Streptomyces, fungi, yeast,animal cells, plant cells, insect cells, and the like. Preferredembodiments of the present invention include chalcone synthase mutantsthat are expressed in E. coli or in plant cells. Said plant cells caneither be in suspension culture or a transgenic plant as furtherdescribed herein.

As stated previously, genes encoding synthases of the present inventioncan be expressed in transgenic plant cells. In order to producetransgenic plants, vectors containing the nucleic acid constructencoding polyketide synthases and mutants thereof are inserted into theplant genome. Preferably, these recombinant vectors are capable ofstable integration into the plant genome. One variable in making atransgenic plant is the choice of a selectable marker. A selectablemarker is used to identify transformed cells against a high backgroundof untransformed cells. The preference for a particular marker is at thediscretion of the artisan, but any of the selectable markers may be usedalong with any other gene not listed herein that could function as aselectable marker. Such selectable markers include aminoglycosidephosphotransferase gene of transposon Tn5 (Aph 11) (which encodesresistance to the antibiotics kanamycin), genes encoding resistance toneomycin or G418, as well as those genes which code for resistance ortolerance to glyphosate, hygromycin, methotrexate, phosphinothricin,imidazolinones, sulfonylureas, triazolophyrimidine herbicides, such aschlorosulfuron, bromoxynil, dalapon, and the like. In addition to aselectable marker, it may be desirable to use a reporter gene. In someinstances a reporter gene may be used with a selectable marker. Reportergenes allow the detection of transformed cells and may be used at thediscretion of the artisan. A list of these reporter genes is provided inK. Wolsing et al., 1988, Ann. Rev. Genetics, 22:421.

Said genes are expressed either by promoters expressing in all tissuesat all times (constitutive promoters), by promoters expressing inspecific tissues (tissue-specific promoters), promoters expressing atspecific stages of development (developmental promoters), and/orpromoter expression in response to a stimulus or stimuli (induciblepromoters). The choice of these is at the discretion of the artisan.

Several techniques exist for introducing foreign genes into plant cells,and for obtaining plants that stably maintain and express the introducedgene. Such techniques include acceleration of genetic material coated ona substrate directly into cells (U.S. Pat. No. 4,945,050 to Comell):Plant cells may also be transformed using Agrobacterium technology (see,for example, U.S. Pat. No. 5,177,010 to University of Toledo, U.S. Pat.No. 5,104,310 to Texas A&M, U.S. Pat. Nos. 5,149,645, 5,469,976,5,464,763, 4,940,838, and 4,693,976 to Schilperoot, European PatentApplications 116718, 290799, 320500 to Max Planck, European PatentApplications 604662,627752 and U.S. Pat. No. 5,591,616 to Japan Tobacco,European Patent Applications 0267159, 0292435 and U.S. Pat. No.5,231,019 to Ciba-Geigy, U.S. Pat. Nos. 5,463,174 and 4,762,785 toCalgene, and U.S. Pat. Nos. 5,004,863 and 5,159,135 to Agracetus). Othertransformation technologies include whiskers technology (see U.S. Pat.Nos. 5,302,523 and 5,464,765 to Zeneca). Electroporation technology hasalso been used to transform plants (see WO 87106614 to Boyce ThompsonInstitute, U.S. Pat. Nos. 5,472,869 and 5,384,253 to Dakalb, and WO92/09696 and WO 93/21335 to Plant Genetic Systems, all which areincorporated by reference). Viral vector expression systems can also beused such as those described in U.S. Pat. Nos. 5,316,931, 5,589,367,5,811,653, and 5,866,785 to BioSource, which are incorporated byreference herein.

In addition to numerous technologies for transforming plants, the typeof tissue that is contacted with the genes of interest may vary as well.Suitable tissue includes, for example, embryonic tissue, callus tissue,hypocotyl, meristem, and the like. Almost all plant tissues may betransformed during de-differentiation using the appropriate techniquesdescribed herein.

In addition, it may be desirable to change the polyketide production ofa polyketide synthase within a plant. For example, it may be beneficialto increase the production of resveratrol in a plant. Resveratrol, thenatural product made by the CHS-related stilbene synthase (STS) enzymes,is an antifungal compound produced in a few families of plants,including pine trees, grapevines, and peanuts. When stilbene synthase isintroduced into plants like tobacco or alfalfa, which normally lack thisenzyme, the transgenic plant becomes resistant to fungal infection (Mol.Plant Microbe Interact. 13(5):551-62, 2000; and Nature 361(6408):153-6,1993). Since STS uses the exact same substrates as CHS, which isubiquitous in higher plants, expression of the STS gene in any of thesespecies should be sufficient to achieve the in vivo biosynthesis ofresveratrol.

Furthermore, resveratrol has also been shown to have a number ofbeneficial medicinal activities, including copper chelation,anti-oxidant scavenging of free radicals, inhibition of both plateletaggregation and lipid peroxidation, anti-inflammation, vasodilation,anti-cancer (Life Sci. 66(8):663-73, 2000), and the like. These effectsof resveratrol contribute to the health benefits of the moderateconsumption of red wine, known as “the French paradox”. Red wine has ahigher resveratrol content than grape juice or white wine, due to theinclusion of the resveratrol-rich grape skins during the fermentationprocess.

Thus, production of resveratrol in plants which lack it is biologicallyuseful for the plant, and medicinally useful for humans who consume theplant. While transgenic introduction of the stilbene synthase gene hasproven effective, enzymes are often best-adapted for expression andstability within their own species. The ability to engineer full orpartial STS activity into a native CHS of a given species confers thebenefits of resveratrol production to that species, while avoiding allof the negative effects of foreign transgene expression.

The mutants of the present invention show that it is possible to mutatea native CHS to a STS-like activity (see FIG. 14). Furthermore, it ispossible to produce the STS product resveratrol to varying degrees withdifferent mutants. Thus, a plant can be manipulated to produce varyinglevels of resveratrol, without eliminating the production of thechalcone product required for viability.

Regardless of the transformation system used, a gene encoding a mutantpolyketide synthase is preferably incorporated into a gene transfervector adapted to express said gene in a plant cell by including in thevector an expression control sequence (plant promoter regulatoryelement). In addition to plant promoter regulatory elements, promoterregulatory elements from a variety of sources can be used efficiently inplant cells to express foreign genes. For example, promoter regulatoryelements of bacterial origin, such as the octopine synthase promoter,the nopaline synthase promoter, the mannopine synthase promoter, and thelike, may be used. Promoters of viral origin, such as the cauliflowermosaic virus (35S and 198) are also desirable. Plant promoter regulatoryelements also include ribulose-1,6-bisphosphate carboxylase smallsubunit promoter, beta-conglycinin promoter, phaseolin promoter, ADHpromoter, heat-shock promoters, tissue specific promoters, and the like.Numerous promoters are available to skilled artisans for use at theirdiscretion.

It should be understood that not all expression vectors and expressionsystems function in the same way to express the mutated gene sequencesof the present invention. Neither do all host cells function equallywell with the same expression system. However, one skilled in the artmay make a selection among these vectors, expression control sequences,and host without undue experimentation and without departing from thescope of this invention.

Once a synthase of the present invention is expressed, the proteinobtained therefrom can be purified so that structural analysis,modeling, and/or biochemical analysis can be performed, as exemplifiedherein. The nature of the protein obtained can be dependent on theexpression system used. For example, genes, when expressed in mammalianor other eukaryotic cells, may contain latent signal sequences that mayresult in glycosylation, phosphorylation, or other post-translationalmodifications, which may or may not alter function. Therefore, apreferred embodiment of the present invention is the expression ofmutant synthase genes in E. coli cells. Once said proteins areexpressed, they can be easily purified using techniques common to theperson having ordinary skill in the art of protein biochemistry, suchas, for example, techniques described in Colligan et al., (1997) CurrentProtocols in Protein Science, Chanda, V. B., Ed., John Wiley & Sons,Inc., which is incorporated by reference herein. Such techniques ofteninclude the use of cation-exchange or anion-exchange chromatography, gelfiltration-size exclusion chromatography, and the like. Anothertechnique that may be commonly used is affinity chromatography. Affinitychromatography can include the use of antibodies, substrate analogs, orhistidine residues (His-tag technology).

Once purified, mutants of the present invention may be characterized byany of several different properties. For example, such mutants may havealtered active site surface charges of one or more charge units. Inaddition, said mutants may have altered substrate specificity or productcapability relative to a non-mutated polyketide synthase.

The present invention allows for the characterization of polyketidesynthase mutants by crystallization followed by X-ray diffraction.Polypeptide crystallization occurs in solutions where the polypeptideconcentration exceeds it solubility maximum (i.e., the polypeptidesolution is supersaturated). Such solutions may be restored toequilibrium by reducing the polypeptide concentration, preferablythrough precipitation of the polypeptide crystals. Often polypeptidesmay be induced to crystallize from supersaturated solutions by addingagents that alter the polypeptide surface charges or perturb theinteraction between the polypeptide and bulk water to promoteassociations that lead to crystallization.

Compounds known as “precipitants” are often used to decrease thesolubility of the polypeptide in a concentrated solution by forming anenergetically unfavorable precipitating layer around the polypeptidemolecules (Weber, Advances in Protein Chemistry, 41:1-36, 1991). Inaddition to precipitants, other materials are sometimes added to thepolypeptide crystallization solution. These include buffers to adjustthe pH of the solution and salts to reduce the solubility of thepolypeptide. Various precipitants are known in the art and include thefollowing: ethanol, 3-ethyl-2-4 pentanediol, and many of thepolyglycols, such as polyethylene glycol.

Commonly used polypeptide crystallization methods include the followingtechniques: batch, hanging drop, seed initiation, and dialysis. In eachof these methods, it is important to promote continued crystallizationafter nucleation by maintaining a supersaturated solution. In the batchmethod, polypeptide is mixed with precipitants to achievesupersaturation, the vessel is sealed, and set aside until crystalsappear. In the dialysis method, polypeptide is retained in a sealeddialysis membrane that is placed into a solution containing precipitant.Equilibration across the membrane increases the polypeptide andprecipitant concentrations thereby causing the polypeptide to reachsupersaturation levels.

In the preferred hanging drop technique (McPherson, J. Biol Chem,6300-6306, 1976), an initial polypeptide mixture is created by adding aprecipitant to a concentrated polypeptide solution. The concentrationsof the polypeptide and precipitants are such that in this initial form,the polypeptide does not crystallize. A small drop of this mixture isplaced on a glass slide that is inverted and suspended over a reservoirof a second solution. The system is then sealed. Typically, the secondsolution contains a higher concentration of precipitant or otherdehydrating agent. The difference in the precipitant concentrationscauses the protein solution to have a higher vapor pressure than thesolution. Since the system containing the two solutions is sealed, anequilibrium is established, and water from the polypeptide mixturetransfers to the second solution. This equilibrium increases thepolypeptide and precipitant concentration in the polypeptide solution.At the critical concentration of polypeptide and precipitant, a crystalof the polypeptide will form.

Another method of crystallization introduces a nucleation site into aconcentrated polypeptide solution. Generally, a concentrated polypeptidesolution is prepared and a seed crystal of the polypeptide is introducedinto this solution. If the concentration of the polypeptide and anyprecipitants are correct, the seed crystal will provide a nucleationsite around which a larger crystal forms. In preferred embodiments, thecrystals of the present invention are formed in hanging drops.

Some proteins may be recalcitrant to crystallization. However, severaltechniques are available to the skilled artisan. Quite often the removalof polypeptide segments at the amino or caroxy terminal end of theprotein is necessary to produce crystalline protein samples. Saidprocedures involve either the treatment of the protein with one ofseveral proteases including trypsin, chymotrypsin, substilisin, and thelike. This treatment often results in the removal of flexiblepolypeptide segments that are likely to negatively affectcrystallization. Alternatively, the removal of coding sequences from theprotein's gene facilitates the recombinant expression of shortenedproteins that can be screened for crystallization.

The crystals so produced have a wide range of uses. For example, highquality crystals are suitable for X-ray or neutron diffraction analysisto determine the three-dimensional structure of a mutant polyketidesynthase and to design additional mutants thereof. In addition,crystallization can serve as a further purification method. In someinstances, a polypeptide or protein will crystallize from aheterogeneous mixture into crystals. Isolation of such crystals byfiltration, centrifugation, etc., followed by redissolving thepolypeptide affords a purified solution suitable for use in growing thehigh-quality crystals needed for diffraction studies. The high-qualitycrystals may also be dissolved in water and then formulated to providean aqueous solution having other uses as desired.

Because synthases may crystallize in more than one crystal form, thestructural coordinates of α-carbons of an active site determined from asynthase or portions thereof, as provided by this invention, areparticularly useful to solve the structure of other crystal forms ofsynthases. Said structural coordinates, as provided herein, may also beused to solve the structure of synthases having α-carbons positionedwithin the active sites in a manner similar to the wild-type, yet havingR-groups that may or may not be identical.

Furthermore, the structural coordinates disclosed herein may be used todetermine the structure of the crystalline form of other proteins withsignificant amino acid or structural homology to any functional domainof a synthase. One method that may be employed for such purpose ismolecular replacement. In this method, the unknown crystal structure,whether it is another crystal form of a synthase, a synthase having amutated active site, or the crystal of some other protein withsignificant sequence and/or structural homology to a polyketide synthasemay be determined using the coordinates given in Table 1. This methodprovides sufficient structural form for the unknown crystal moreefficiently than attempting to determine such information ab initio. Inaddition, this method can be used to determine whether or not a givenpolyketide synthase in question falls within the scope of thisinvention.

As further disclosed herein, polyketide synthases and mutants thereofmay be crystallized in the presence or absence of substrates andsubstrate analogs. The crystal structures of a series of complexes maythen be solved by molecular replacement and compared to that of thewild-type to assist in determination of suitable replacements forR-groups within the active site, thus making synthase mutants accordingto the present invention.

All mutants of the present inventions may be modeled using theinformation disclosed herein without necessarily having to crystallizeand solve the structure for each and every mutant. For example, oneskilled in the art may use one of several specialized computer programsto assist in the process of designing synthases having mutated activesites relative to the wild-type. Examples of such programs include: GRID(Goodford, 1985, J. Mod. Chem.:28:849-857), MCSS (Miranker and Karplus,1991, Proteins: Structure, Function and Genetics, 11:29-34); AUTODOCK(Goodsell and Olsen, 1990, Proteins. Structure, Fumtion, and Genetics,8:195-202); and DOCK (Kuntz et al., 1982, J. Mol Biol:161:269-288), andthe like, as well as those discussed in the Examples below. In addition,specific computer programs are also available to evaluate specificsubstrate-active site interactions and the deformation energies andelectrostatic interactions resulting therefrom. MODELLER is a computerprogram often used for homology or comparative modeling of thethree-dimensional structure of a protein. A. Saii & T. L. Blundell. J.Mol. Biol. 234:779-815, 1993. A sequence to be modeled is aligned withone or more known related structures and the MODELLER program is used tocalculate a full-atom model, based on optimum satisfaction of spatialrestraints. Such restraints can include, inter alia, homologousstructures, site-directed mutagenesis, fluorescence spectroscopy, NMRexperiments, or atom-atom potentials of mean force.

The present invention enables polyketide synthase mutants to be made andthe crystal structure thereof to be solved. Moreover, by virtue of thepresent invention, the location of the active site and the interface ofsubstrate therewith permit the identification of desirable R-groups formutagenesis.

The three-dimensional coordinates of the polyketide synthase providedherein may additionally be used to predict the activity and or substratespecificity of a protein whose primary amino acid sequence suggests thatit may have polyketide synthase activity. The family of CHS-relatedenzymes is defined, in part, by the presence of four highly conservedamino acid residues, Cys₁₆₄, Phe₂₁₅, His₃₀₃, and Asn₃₃₆. More than 400enzymes having these conserved residues have been identified to date,including several bacterial proteins. The functions, substrates, andproducts of many of these enzymes remains unknown. However, by employingthe three-dimensional coordinates disclosed herein and computer modelingprograms, structural comparisons of CHS can be made with a putativeenzyme. Similarities and differences between the two would provide theskilled artisan with information regarding the activity and/or substratespecificity of the putative enzyme. This procedure is demonstrated inthe Examples section below.

Thus, in another embodiment of the invention, there is provided a methodof predicting the activity and/or substrate specificity of a putativepolyketide synthase comprising (a) generating a three-dimentionalrepresentation of a known polyketide synthase using three-dimentionalcoordinate data, (b) generating a predicted three-dimentionalrepresentation of a putative polyketide synthase, and (c) comparing therepresentation of the known polyketide synthase with the representationof the putative polyketide synthase, wherein the similarities and/ordifferences between the two representations are predictive of activityand/or substrate specificity of the putative polyketide synthase.

In a further embodiment of the present invention, there is also provideda method of identifying a potential substrate of a polyketide synthasecomprising (a) defining the active site of the polyketide synthase basedon the atomic coordinates of said polyketide synthase, (b) identifying apotential substrate that fits the defined active site, and (c)contacting the polyketide synthase with the potential substrate of (b)and determining the activity thereon. Techniques for computer modelingand structural comparisons similar to those described herein forpredicting putative polyketide synthase activity and/or substratespecificity can be used to identify novel substrates for polyketidesynthases.

In addition, the structural coordinates and three-dimensional modelsdisclosed herein can be used to design or identify polyketide synthaseinhibitors. Using the modeling techniques disclosed herein, potentialinhibitor structures can be modeled with the polyketide synthase activesite and those that appear to interact therewith can subsequently betested in activity assays in the presence of substrate.

Methods of using crystal structure data to design binding agents orsubstrates are known in the art. Thus, the crystal structure dataprovided herein can be used in the design of new or improved inhibitors,substrates or binding agents. For example, the synthase polypeptidecoordinates can be superimposed onto other available coordinates ofsimilar enzymes to identify modifications in the active sites of theenzymes to create novel products of enzymatic activity or to modulatepolyketide synthesis. Alternatively, the synthase polypeptidecoordinates can be superimposed onto other available coordinates ofsimilar enzymes which have substrates or inhibitors bound to them togive an approximation of the way these and related substrates orinhibitors might bind to a synthase. Alternatively, computer programsemployed in the practice of rational drug design can be used to identifycompounds that reproduce interaction characteristics similar to thosefound between a synthase polypeptide and a co-crystallized substrate.Furthermore, detailed knowledge of the nature of binding siteinteractions allows for the modification of compounds to alter orimprove solubility, pharmacokinetics, etc. without affecting bindingactivity.

Computer programs are widely available that are capable of carrying outthe activities necessary to design agents using the crystal structureinformation provided herein. Examples include, but are not limited to,the computer programs listed below:

-   -   CATALYST DATABASES™—an information retrieval program accessing        chemical databases such as BioByte Master File, Derwent WDI and        ACD;    -   CATALYST/HYPO™—generates models of compounds and hypotheses to        explain variations of activity with the structure of drug        candidates;    -   LUDI™—fits molecules into the active site of a protein by        identifying and matching complementary polar and hydrophobic        groups;    -   LEAPFROG™—“grows” new ligands using a genetic algorithm with        parameters under the control of the user.

In addition, various general purpose machines may be used with programswritten in accordance with the teachings herein, or it may be moreconvenient to construct more specialized apparatus to perform theoperations. However, preferably the embodiment is implemented in one ormore computer programs executing on programmable systems each comprisingat least one processor, at least one data storage system (includingvolatile and non-volatile memory and/or storage elements), at least oneinput device, and at least one output device. The program is executed onthe processor to perform the functions described herein.

Each such program may be implemented in any desired computer language(including machine, assembly, high level procedural, object orientedprogramming languages, or the like) to communicate with a computersystem. In any case, the language may be a compiled or interpretedlanguage. The computer program will typically be stored on a storagemedia or device (e.g., ROM, CD-ROM, or magnetic or optical media)readable by a general or special purpose programmable computer, forconfiguring and operating the computer when the storage media or deviceis read by the computer to perform the procedures described herein. Thesystem may also be considered to be implemented as a computer-readablestorage medium, configured with a computer program, where the storagemedium so configured causes a computer to operate in a specific andpredefined manner to perform the functions described herein.

Embodiments of the invention include systems (e.g., internet basedsystems), particularly computer systems which store and manipulate thecoordinate and sequence information described herein. One example of acomputer system 100 is illustrated in block diagram form in FIG. 9. Asused herein, “a computer system” refers to the hardware components,software components, and data storage components used to analyze thecoordinates and sequences as set forth in one or more of Accession Nos.1BI5, 1D6F, 1D61, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, andAppendix A. The computer system 100 typically includes a processor forprocessing, accessing and manipulating the sequence data. The processor105 can be any well-known type of central processing unit, such as, forexample, the Pentium III from Intel Corporation, or similar processorfrom Sun, Motorola, Compaq, AMD or International Business Machines.

Typically the computer system 100 is a general purpose system thatcomprises the processor 105 and one or more internal data storagecomponents 110 for storing data, and one or more data retrieving devicesfor retrieving the data stored on the data storage components. A skilledartisan can readily appreciate that any one of the currently availablecomputer systems are suitable.

In one particular embodiment, the computer system 100 includes aprocessor 105 connected to a bus which is connected to a main memory 115(preferably implemented as RAM) and one or more internal data storagedevices 110, such as a hard drive and/or other computer readable mediahaving data recorded thereon. In some embodiments, the computer system100 further includes one or more data retrieving device 118 for readingthe data stored on the internal data storage devices 110.

The data retrieving device 118 may represent, for example, a floppy diskdrive, a compact disk drive, a magnetic tape drive, or a modem capableof connection to a remote data storage system (e.g., via the internet)etc. In some embodiments, the internal data storage device 110 is aremovable computer readable medium such as a floppy disk, a compactdisk, a magnetic tape, etc. containing control logic and/or datarecorded thereon. The computer system 100 may advantageously include orbe programmed by appropriate software for reading the control logicand/or the data from the data storage component once inserted in thedata retrieving device.

The computer system 100 includes a display 120 which is used to displayoutput to a computer user. It should also be noted that the computersystem 100 can be linked to other computer systems 125 a-c in a networkor wide area network to provide centralized access to the computersystem 100.

Software for accessing and processing the coordinate and sequencesdescribed herein, (such as search tools, compare tools, and modelingtools etc.) may reside in main memory 115 during execution.

For the first time, the present invention permits the use of moleculardesign techniques to design, select and synthesize novel enzymes,chemical entities and compounds, including inhibitory compounds, capableof binding to a polyketide synthase polypeptide (e.g., a chalconesynthase polypeptide), in whole or in part.

One approach enabled by this invention, is to use the structurecoordinates as set forth in one or more of Accession Nos. 1BI5 (SEQ IDNO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69),1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQID NO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A(SEQ ID NO:65), Appendix B (SEQ ID NO:66) and Appendix C (SEQ ID NO:67)to design new enzymes capable of synthesizing novel and knownpolyketides. For example, polyketide synthases (PKSs) generate moleculardiversity in their products by utilizing different starter molecules andby varying the final size of the polyketide chain. The structuralcoordinates disclosed herein allow the elucidation of the nature bywhich PKSs achieve starter molecule selectivity and control polyketidechain length. For example, by comparing the structure of chalconesynthase, which yields a tetraketide product to 2-pyrone synthases whichforms a triketide product the invention demonstrated that 2-pyronesynthase maintains a smaller initiation/elongation cavity. Accordingly,generation of a chalcone synthase mutant with an active site stericallyanalogous to 2-pyrone synthase results in the synthesis of a polyketideproduct of a different size. As discussed more fully below, thisinvention allows for the strategic development and biosynthesis of morediverse polyketides and demonstrates a structural basis for control ofpolyketide chain length in other PKSs. In addition, the structuralcoordinates allow for the development of substrates or binding agentsthat bind to the polypeptide and alter the physical properties of thecompounds in different ways, e.g., solubility.

In another approach a polyketide synthase polypeptide crystal is probedwith molecules composed of a variety of different chemical entities todetermine optimal sites for interaction between candidate bindingmolecules (e.g., substrates) and the polyketide synthase (e.g., chalconesynthase).

In another embodiment, an approach made possible and enabled by thisinvention, is to screen computationally small molecule data bases forchemical entities or compounds that can bind in whole, or in part, to apolyketide synthase polypeptide or fragment thereof. In this screening,the quality of fit of such entities or compounds to the binding site maybe judged either by shape complementarity or by estimated interactionenergy. Meng, E. C. et al., J. Comp. Chem., 13:505-524 (1992).

Because chalcone synthase is a highly representative member of a familyof polyketide synthase polypeptides, many of which have similarfunctional activity, the structure coordinates of chalcone synthase, orportions thereof, as provided by this invention are particularly usefulto solve the structure, function or activity of other crystal forms ofpolyketide synthase molecules. They may also be used to solve thestructure of a polyketide synthase or a chalcone synthase mutant.

One method that may be employed for this purpose is molecularreplacement. In this method, the unknown crystal structure, whether itis another polyketide synthase crystal form, a polyketide synthase orchalcone synthase mutant, or a polyketide synthase complexed with asubstrate or other molecule, or the crystal of some other protein withsignificant amino acid sequence homology to any polyketide synthasepolypeptide, may be determined using the structure coordinates asprovided in one or more of Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ IDNO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69),1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68, Table 1, Appendix A (SEQ IDNO:65), Appendix B (SEQ ID NO:66) or Appendix C (SEQ ID NO:67). Thismethod will provide an accurate structural form for the unknown crystalmore quickly and efficiently than attempting to determine suchinformation ab initio.

In addition, in accordance with the present invention, a polyketidesynthase or chalcone synthase polypeptide mutant maybe crystallized inassociation or complex with known polyketide synthase binding agents,substrates, products or inhibitors. The crystal structures of a seriesof such complexes may then be solved by molecular replacement andcompared with that of wild-type polyketide synthase molecules. Potentialsites for modification within the synthase molecule may thus beidentified. This information provides an additional tool for determiningthe most efficient binding interactions between a polyketide synthaseand a chemical entity, substrate, product or compound.

All of the complexes referred to above may be studied using well-knownX-ray diffraction techniques and may be refined to 2-3 Å resolutionX-ray data to an R value of about 0.20 or less using computer software,such as X-PLOR (Yale University, 1992, distributed by MolecularSimulations, Inc.). See, e.g., Blundel & Johnson, supra; Methods inEnzymology, vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press(1985). This information may thus be used to optimize known classes ofpolyketide synthase substrates or binding agents (e.g., inhibitors), andto design and synthesize novel classes of polyketide synthases,substrates, and binding agents (e.g. inhibitors).

The design of substrates, compounds or binding agents that bind to orinhibit a polyketide synthase polypeptide according to the inventiongenerally involves consideration of two factors. First, the substrate,compound or binding agent must be capable of physically and structurallyassociating with a polyketide synthase molecule. Non-covalent molecularinteractions important in the association of a polyketide synthase witha substrate include hydrogen bonding, van der Waals and hydrophobicinteractions, and the like.

Second, the substrate, compound or binding agent must be able to assumea conformation that allows it to associate with a polyketide synthasemolecule. Although certain portions of the substrate, compound orbinding agent will not directly participate in this association, thoseportions may still influence the overall conformation of the molecule.This, in turn, may have a significant impact on potency. Suchconformational requirements include the overall three-dimensionalstructure and orientation of the chemical entity or compound in relationto all or a portion of the binding site, e.g., active site or accessorybinding site of a polyketide synthase (e.g., a chalcone synthasepolypeptide), or the spacing between functional groups of a substrate orcompound comprising several chemical entities that directly interactwith a polyketide synthase.

The potential binding effect of a substrate or chemical compound on apolyketide synthase or the activity a newly synthesized or mutatedpolyketide synthase might have on a known substrate may be analyzedprior to its actual synthesis and testing by the use of computermodeling techniques. For example, if the theoretical structure of thegiven substrate or compound suggests insufficient interaction andassociation between it and a polyketide synthase, synthesis and testingof the compound may be obviated. However, if computer modeling indicatesa strong interaction, the molecule may then be tested for its ability tobind to, initiate catalysis or elongation of a polyketide by apolyketide synthase. Methods of assaying for polyketide synthaseactivity are known in the art (as identified and discussed herein).Methods for assaying the effect of a newly created polyketide synthaseor a potential substrate or binding agent can be performed in thepresence of a known binding agent or polyketide synthase. For example,the effect of the potential binding agent can be assayed by measuringthe ability of the potential binding agent to compete with a knownsubstrate.

A mutagenized synthase, novel synthase, substrate or other bindingcompound of an polyketide synthase may be computationally evaluated anddesigned by means of a series of steps in which chemical entities orfragments are screened and selected for their ability to associate withbinding pockets or other areas of the polyketide synthase.

One skilled in the art may use one of several methods to screen chemicalentities or fragments for their ability to associate with a polyketidesynthase and more particularly with the individual binding pockets of achalcone synthase polypeptide. This process may begin by visualinspection of, for example, the active site on the computer screen basedon the coordinates in one or more of Accession Nos. 1BI5 (SEQ ID NO:69),1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ IDNO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A(SEQ ID NO:65), Appendix B (SEQ ID NO:66) or Appendix C (SEQ ID NO:67).Selected fragments or substrates or chemical entities may then bepositioned in a variety of orientations, or docked, within an individualbinding pocket of a polyketide synthase. Docking may be accomplishedusing software such as Quanta and Sybyl, followed by energy minimizationand molecular dynamics with standard molecular mechanics forcefields,such as CHARMM and AMBER.

Specialized computer programs may also assist in the process ofselecting fragments or chemical entities. These include:

1. GRID (Goodford, P. J., “A Computational Procedure for DeterminingEnergetically Favorable Binding Sites on Biologically ImportantMacromolecules”, J. Med. Chem., 28:849-857 (1985)). GRID is availablefrom Oxford University, Oxford, UK.

2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of BindingSites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure.Function and Genetics, 11:29-34 (1991)). MCSS is available fromMolecular Simulations, Burlington, Mass.

3. AUTODOCK (Goodsell, D. S. and A. J. Olsen, “Automated Docking ofSubstrates to Proteins by Simulated Annealing”, Proteins: Structure.Function, and Genetics, 8:195-202 (1990)). AUTODOCK is available fromScripps Research Institute, La Jolla, Calif.

4. DOCK (Kuntz, I. D. et al, “A Geometric Approach toMacromolecule-Ligand Interactions”, J. Mol. Biol., 161:269-288 (1982)).DOCK is available from University of California, San Francisco, Calif.

Once suitable substrates, chemical entities or fragments have beenselected, they can be assembled into a single polypeptide, compound orbinding agent (e.g., an inhibitor). Assembly may be performed by visualinspection of the relationship of the fragments to each other on thethree-dimensional image displayed on a computer screen in relation tothe structure coordinates of the molecules as set forth in one or moreof Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ IDNO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69),1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69), 1CGZ (SEQ ID NO:69). 1EE0 (SEQID NO:68), Table 1, Appendix A (SEQ ID NO:65), Appendix B (SEQ ID NO:66)or Appendix C (SEQ ID NO:67). This would be followed by manual modelbuilding using software such as Quanta or Sybyl.

Useful programs to aid one of skill in the art in connecting theindividual chemical entities or fragments include:

1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate theStructure-Derived Design of Biologically Active Molecules”. In“Molecular Recognition in Chemical and Biological Problems”, SpecialPub., Royal Chem. Soc., 78, pp. 182-196 (1989)). CAVEAT is availablefrom the University of California, Berkeley, Calif.

2. 3D Database systems such as MACCS-3D (MDL Information Systems, SanLeandro, Calif.). This area is reviewed in Martin, Y. C., “3D DatabaseSearching in Drug Design”, J. Med. Chem., 35:2145-2154 (1992)).

3. HOOK (available from Molecular Simulations, Burlington, Mass.).

In addition to the method of building or identifying novel enzymes or apolyketide synthase substrate or binding agent in a step-wise fashionone fragment or chemical entity at a time as described above,substrates, inhibitors or other polyketide synthase interactions may bedesigned as a whole or “de novo” using either an empty active site oroptionally including some portion(s) of known substrates, binding agentsor inhibitors. These methods include:

1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method for theDe Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design,6:61-78 (1992)). LUDI is available from Biosym Technologies, San Diego,Calif.

2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47:8985 (1991)).LEGEND is available from Molecular Simulations, Burlington, Mass.

3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordancewith this invention. See, e.g., Cohen, N. C. et al., “Molecular ModelingSoftware and Methods for Medicinal Chemistry”, J. Med. Chem., 33:883-894(1990). See also, Navia, M. A. and M. A. Murcko, “The Use of StructuralInformation in Drug Design”, Current Opinions in Structural Biology,2:202-210 (1992).

Once a substrate, compound or binding agent has been designed orselected by the above methods, the efficiency with which that substrate,or binding agent may bind to a polyketide synthase may be tested andoptimized by computational evaluation.

A substrate or compound designed or selected as a polyketide bindingagent may be further computationally optimized so that in its boundstate it would preferably lack repulsive electrostatic interaction withthe target site. Such non-complementary (e.g., electrostatic)interactions include repulsive charge-charge, dipole-dipole andcharge-dipole interactions. Specifically, the sum of all electrostaticinteractions between the binding agent and the polyketide synthase whenthe binding agent is bound to the synthase, preferably make a neutral orfavorable contribution to the enthalpy of binding.

Specific computer software is available in the art to evaluate compounddeformation energy and electrostatic interaction. Examples of programsdesigned for such uses include: Gaussian 92, revision C (M. J. Frisch,Gaussian, Inc., Pittsburgh, Pa., 1992); AMBER, version 4.0 (P. A.Kollman, University of California at San Francisco, 1994); QUANTA/CHARMM(Molecular Simulations, Inc., Burlington, Mass. 1994); and InsightII/Discover (Biosysm Technologies Inc., San Diego, Calif., 1994). Theseprograms maybe implemented, for example, using a Silicon Graphicsworkstation, IRIS 4D/35 or IBM RISC/6000 workstation model 550. Otherhardware systems and software packages will be known to those skilled inthe art of which the speed and capacity are continually modified

Once a polyketide synthase, polyketide synthase substrate or polyketidesynthase binding agent has been selected or designed, as describedabove, substitutions may then be made in some of its atoms or sidegroups in order to improve or modify its binding properties. Generally,initial substitutions are conservative, e.g., the replacement group willhave approximately the same size, shape, hydrophobicity and charge asthe original group. Such substituted chemical compounds may then beanalyzed for efficiency of fit to a polyketide synthase substrate or fitof a modified substrate to a polyketide synthase having a structuredefined by the coordinates in one or more of Accession Nos. 1BI5, 1D6F,1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, 1EE0, Table 1, Appendix A,Appendix B, or Appendix C, by the same computer methods described,above.

Conserved regions of the polyketide family synthases lend themselves tothe methods and compositions of the invention. For example, pyronesynthase and chalcone synthase have conserved residues present withintheir active sites (as described more fully below). Accordingly,modification to the active site of chalcone synthase or a chalconesynthase substrate can be extrapolated to other conserved members of thepolyketide family of synthases such as, for example, pyrone synthase.

Functional fragments of polyketide synthase polypeptides such as, forexample, fragments of chalcone synthase can be designed based on thecrystal structure and atomic coordinates described herein. Fragments ofa chalcone synthase polypeptide and the fragment's corresponding atomiccoordinates can be used in the modeling described herein. In addition,such fragments may be used to design novel substrates or modified activesites to create new diverse polyketides.

In one embodiment of the present invention, the crystal structure andatomic coordinates allow for the design of novel polyketide synthasesand novel polyketide synthase substrates. The development of newpolyketide synthases will lead to the development a biodiverse repetoirof polyketides for use as antibiotics, anti-cancer agents, anti-fungalagents and other therapeutic agents as described herein or known in theart. In vitro assay systems for production and determination of activityare known in the art. For example, antibiotic activities of novelpolyketides can be measured by any number of anti-microbial techniquescurrently used in hospitals and laboratories. In addition, anticanceractivity can be determined by contacting cells having a cellproliferative disorder with a newly synthesized polyketide and measuringthe proliferation or apoptosis of the cells before and after contactwith the polyketide. Specific examples of apoptosis assays are providedin the following references: Lymphocyte: C. J. Li et al., Science,268:429-431, 1995; D. Gibellini et al., Br. J. Haematol. 89:24-33, 1995;S. J. Martin et al., J. Immunol. 152:330-42, 1994; C. Terai et al., J.Clin Invest. 87:1710-5, 1991; J. Dhein et al., Nature 373:438441, 1995;P. D. Katsikis et al., J. Exp. Med. 1815:2029-2036, 1995; Michael O.Westendorp et al., Nature 375:497, 1995; DeRossi et ad, Virology198:234-44, 1994. Fibroblasts: H. Vossbeck et al., Int. J. Cancer61:92-97, 1995; S. Gomppi et al., Oncogene 9:1537-44, 1994; A. Fernandezet al., Oncogene 9:2009-17, 1994; E. A. Harrington et al., Embo J.13:3286-3295, 1994; N. Itoh et al., J. Biol. Chem. 268:10932-7, 1993.Neuronal Cells: G. Melino et al., Mol. Cell. Biol. 14:6584-6596, 1994;D. M. Rosenbaum et al., Ann. Neurol. 36:864-870, 1994; N. Sato et al.,J. Neurobiol 25:1227-1234, 1994; G. Ferrari et al., J. Neurosci.1516:2857-2866, 1995; A. K. Talley et al., Mol. Cell Biol.1585:2359-2366, 1995; A. K. Talley et al., Mol. and Cell. Biol.15:2359-2366, 1995; G. Walkinshaw et al., J. Clin. Invest. 95:2458-2464,1995. Insect Cells: R. J. Clem et al., Science 254:1388-90, 1991; N. E.Crook et al., J. Virol. 67:2168-74, 1993; S. Rabizadeh et al., J.Neurochem. 61:2318-21, 1993; M. J. Birnbaum et al., J. Virol 68:2521-8,1994; R. J. Clem et al., Mol. Cell. Biol. 14:5212-5222, (1994). Otherassays are well within the ability of those of skill in the art.

Product of novel polyketides or polyketide synthases can be carried outin culture. For example, mammalian expression constructs carryingpolyketide synthases can be introduced into various cell lines such asCHO, 3T3, HL60, Rat-1, or Jurkart cells, for example. In addition, SF21insect cells may be used in which case the polyketide synthase gene isexpressed using an insect heat shock promotor.

In another embodiment of the present invention, there is provided amethod of designing a mutant polyketide synthese. The method includecomparing a crystal structure of a wild type polyketide synthase withthe crystal structure of a second polyketide synthase and substitutingone or more animo acids with the amino acid residues at homologouspositions in the second polyketide synthase. Invention methods can guidethe required areas or active sites, and second tier interaction residuesfor synthase activity. Such areas can be mutated to modify one synthaseto resemble another synthase, thereby allowing production of a productnot typically synthesized by the wild type enzyme.

In another embodiment of the present invention, once a novel substrateor binding agent is developed by the computer methodology discussedabove, the invention provides a method for determining the ability ofthe substrate or agent to be acted upon by a polyketide synthase. Themethod includes contacting components comprising the substrate or agentand a polyketide synthase polypeptide, or a recombinant cell expressinga polyketide synthase polypeptide, under conditions sufficient to allowthe substrate or agent to interact and determining the affect of theagent on the activity of the polypeptide. The term “affect”, as usedherein, encompasses any means by which protein activity can bemodulated, and includes measuring the interaction of the agent with thepolyketide synthase molecule by physical means including, for example,fluorescence detection of the binding of an agent to the polypeptide.Such agents can include, for example, polypeptides, peptidomimetics,chemical compounds, small molecules, substrates and biologic agents asdescribed herein. Examples of small molecules include but are notlimited to small peptides or peptide-like molecules.

Contacting or incubating includes conditions which allow contact betweenthe test agent or substrate and a polyketide synthase or modifiedpolyketide synthase polypeptide or a cell expressing a polyketidesynthase or modified polyketide synthase polypeptide. Contactingincludes in solution and in solid phase. The substrate or test agent mayoptionally be a combinatorial library for screening a plurality ofsubstrates or test agents. Agents identified in the method of theinvention can be further evaluated by chromatography, cloning,sequencing, and the like.

Although methods and materials similar or equivalent to those describedherein can be used to practice the invention, suitable methods andmaterials are described below. All publications, patent applications,patents and other references mentioned herein are incorporated byreference in their entirety. The invention is described in greaterdetail by reference to the following non-limiting examples.

EXAMPLES

Mutagenesis, expression, and purification. Alfalfa CHS2 (SEQ ID NO:1)cDNA (Junghans, H., et al., Plant Mol. Biol. 22:239-253, 1993) wassubeloned into pHIS8 plasmid vector derived from pET-28a(+) (Novagen).PCR-based mutagenesis using the QuikChange system (Stratagene) generatedthe various mutants including C₁₆₄S, C₁₆₄D, H₃₀₃A, H₃₀₃Q, H₃₀₃D, H₃₀₃T,N₃₃₆A, N₃₃₆D, N₃₃₆Q, N₃₆₆H, F₂₁₅S, F₂₁₅Y and F215W (see SEQ ID NO:1).N-teminal His8-tagged CHS (see SEQ ID NO:1) was expressed in BL21 (DE3)E. coli cells. Cells were harvested and lysed by sonication. His-taggedCHS (see SEQ ID NO:1) was purified from bacterial sonicates using aNI-NTA (Qiagen) column. Thrombin digest removed the His-tag and theprotein was passed over another NI-NTA column and abenzamidine-Sepharose (Pharmacia) column. The final purification stepused a Superdex 200 16/60 (Pharmacia) column.

Crystallization. CHS crystals (wild-type and C₁₆₄S mutant; see SEQ IDNO:1) were grown by vapor diffusion at 4° C. in 2 μl drops containing a1:1 mixture of 25 mg/ml protein and crystallization buffer (2.2-2.4 Mammoniumsulfate and 0.1 M PIPES, pH 6.5) in the presence or absence of 5mM DIT. Prior to freezing at 105° K, crystals were stabilized in 40%(v/v) PEG400, 0.1 M PIPES (pH 6.5), and 0.050-0.075 M ammonium sulfate.This cryoprotectant was used for heavy atom soaks. Likewise, allsubstrate and product analog complexes were obtained by soaking crystalsin cryoprotectant containing 10-20 mM of the compound.

STS from Pinus sylvestris (SEQ ID NO:65) was crystallized using 13-14%PEG 8000, 0.3M ammonium acetate, 0.1M HEPES buffer (pH 7.4) at 4° C.Crystals were soaked for 60 seconds in the same solution plus 10%glycerol.

STS from Arachis hypogaea (SEQ ID NO:66) was crystallized using 14% PEG8000, 0.1M MOPSO buffer (pH 7.0), with 3% ethylene glycol at 4° C.Crystals were soaked for 30 seconds in the same solution plus 10%ethylene glycol. 18×CHS mutant (SEQ ID NO:67) was crystallized using 21%PEG 8000, 0.3M ammonium acetate, 0.1M HEPES buffer (pH 7.5) at 4° C.Crystals were soaked for 60 seconds in the same solution plus 10%glycerol.

Data Collection and Processing, X-ray diffraction data were collected at105° K using a DIP2000 imaging plate system (Mac-Science Corporation,Japan) and CuK radiation produced by a rotating anode operated at 45 kVand 100 mA and equipped with double focusing Pt/Ni coated mirrors.Native CHS crystals belong to space group P3₂21 with unit celldimensions of a=b=97.54 Å; c=65.52 Å with a single monomer perasymmetric unit. Data were indexed and integrated using DENZO(Otwinowski & Minor, Meth. Enzymol. 276:307-326, 1997) and scaled withSCALEPACK (Otwinowski & Minor, Meth. Enzymol. 276:307-326, 1997). Theheavy atom derivative datasets were scaled against the native datasetwith SCALEIT (CCP4 Suite: Programs for protein crystallography, ActaCrystallogr. D 50:760-763, 1994).

Structure determination. MIRAS was used to solve the structure of nativeCHS (SEQ ID NO:1) using native data set 1 (1.8 Å). Initial phasing wasperformed with derivative datasets including reflections to 2.3 Åresolution. Heavy atom positions for the Hg(OAc)₂ derivative wereestimated by inspection of difference Patterson maps using the programXTALVIEW (McRee, J. Mci. Graph. 10:44-46, 1992) and initially refinedwith MLPHARE (Otwinowski, Z. in CCP4 Proc. 80-88, Daresbury Laboratory,Warrington, UK, 1991). Heavy atom positions for the additionalderivative data sets were determined by difference Fourier analysisusing phases calculated from the Hg(OAc)₂ data set and the Hg positions.These sites were confirmed by inspection of difference Patterson maps.Final refinement of heavy atom parameters, identification of minor heavyatom binding sites, and phase-angle calculations were performed with theprogram SHARP (de La Fortelle, & Bricogne, Meth. Enzymol. 276:472-494,1997). MIRAS phases were improved and extended to 1.8 Å by solventflipping using the CCP4 program SOLOMON (Abrahams and Leslie, ActaCrystallogr. D 52:30-42, 1996).

Model building and refinement The program O (Jones, et al., ActaCrystallogr. D 49:148-157, 1993) was used for model building andgraphical display of the molecules and electron-density maps. Theexperimental map for the native 1 dataset at 1.8 Å was of high qualityand allowed unambiguous modeling of residues 3 to 389. The model wasfirst refined with REFMAC (Murshudov, et al., Acta Crystallogr. D53:240-255, 1997) and ARP (Lamzin and Wilson, Acta Crystallogr. D49:129-147, 1993) against the native 1 dataset. This was followed bymanual adjustments using I2F_(o)-F_(c)1 difference maps. Water moleculesintroduced by ARP were edited using the I2F_(o)-F_(c)1 and IF_(o)-F_(c)1maps. A second refinement with SHELX-97 (Sheldrick & Schneider, Meth.Enzymol. 277:319-343, 1997) was then carried out against the native 2data set to 1.56 Å resolution. Structures of CHS complexed withnaringenin and resveratrol and the C₁₆₄S mutant complexed with malonyl-and hexanoyl-CoA were obtained using difference Fourier methods and wererefined with REFMAC and ARP. All structures were checked with PROCHECK(Laskowski, et al., J. Appl Crystallogr. 26:283-291, 1993). 91.3% of theresidues in CHS are in the most favored regions of the Ramachandranplot, 8.4% in the additional allowed region, and 0.3% in the generouslyallowed region.

Three Dimensional Structure Determination and Description

Recombinant alfalfa CHS2 was expressed in E. coli, affinity purifiedusing an N-terminal poly-His linker, and crystallized. The structure ofwild-type CHS was determined using multiple isomorphous replacementsupplemented with anomalous scattering (MIRAS). The final 1.56 Åresolution apoenzyme model of CHS included 2982 protein atoms and 355water molecules. In addition, the structures of a series of complexeswere obtained by difference Fourier analysis. First, a crystal of amutant (C₁₆₄S) was soaked with malonyl-CoA. This mutant retains limitedcatalytic activity, and the resulting acetyl-CoA complex yields insighton the decarboxylation reaction. The same mutant was also complexed withhexanoyl-CoA to mimic the structure of a linear polyketide-CoA reactionintermediate. Finally, two product analogs, naringenin and resveratrol(see FIG. 1) were complexed with CHS to provide information on how theenzyme governs sequential addition of acetates to the coumaroyl moietyand how CHS controls the stereochemistry of the polyketide cyclizationreaction. In plants, chalcone isomerase rapidly and stereospecificallyconverts chalcone to naringenin ((−)(2S)-5,7,4′-trihydroxyflavanone)through an additional ring closure. This reaction also occurs at aslower rate and non-stereospecifically in solution. As such, naringeninprovides a suitable mimic of the CHS reaction product. Finally, sinceSTS uses the same substrates as CHS but a different cyclization pathwayfor the biosynthesis of resveratrol, resveratrol was also soaked intoCHS to investigate the structural features governing cyclization of thesame substrates into two different products.

CHS functions as a homodimer of two 42 kDa polypeptides. The structureof CHS revealed that the enzyme forms a symmetric dimer with eachmonomer related by a 2-fold crystallographic axis (see FIG. 2). Thedimer interface buries approximately 1580 Å² with interactions occurringalong a fairly flat surface. Two distinct structural features delineatethe ends of this interface. First, the N-terminal helix of monomer Aentwines with the corresponding helix of monomer B. Second, a tight loopcontaining a cis-peptide bond between Met₁₃₇ and Pro₁₃₈ exposes themethionine sidechain as a knob on the monomer surface. Across theinterface, Met₁₃₇ protrudes into a hole found in the surface of theadjoining monomer to form part of the cyclization pocket.

Each CHS monomer consists of two structural domains. The upper domainexhibits an xBxBx pseudo-symmetric motif originally observed in thiolasefrom Saccharomyces cerevisiae (Mathieu, et al, Structure 2:797-808,1994). The upper domains of CHS and thiolase are superimposeable with ar.m.s. deviation of 3.3 Å for 266 equivalent C-atoms. Both enzymes use acysteine as a nucleophile and shuttle reaction intermediates via CoAmolecules. However, CHS condenses a p-coumaroyl- and three malonyl-CoAmolecules through an iterative series of reactions, whereas thiolasegenerates two acetyl-CoA molecules from acetoacetyl-CoA and free CoA.The drastic structural differences in the lower domain of CHS create alarger active site than that of thiolase and provide space for thepolyketide reaction intermediates required for chalcone formation.

The CHS homodimer contains two functionally independent active sites.Consistent with this information, bound CoA thioesters and productanalogs occupy both active sites of the homodimer in the CHS complexstructures. These structures identify the location of the active site atthe cleft between the upper and lower domains of each monomer. Eachactive site consists almost entirely of residues from a single monomerwith Met₁₃₇ from the adjoining monomer being the only exception. Thereare remarkably few chemically reactive residues in the active site. Fourresidues conserved in all the known CHS-related enzymes (Cys₁₆₄, Phe₂₁₅,His₃₀₃, and Asn₃₃₆) define the active site. Cys₁₆₄ apparently serves asthe nucleophile and as the attachment site for polyketide intermediatesas previously suggested for both CHS and STS (Lanz, et al, J. Biol.Chem. 266:9971-9976, 1991). His₃₀₃ most likely acts as a general baseduring the generation of a nucleophilic thiolate anion from Cys₁₆₄,since the Nγ of His₃₀₃ is within hydrogen bonding distance of the sulfurof Cys₁₆₄. Phe₂₁₅ and Asn₃₃₆ may function in the decarboxylationreaction, as discussed below. Topologically, three interconnectedcavities intersect with these four residues and form the active sitearchitecture of CHS. These cavities include a CoA-binding tunnel, acoumaroyl-binding pocket, and a cyclization pocket.

The CoA-binding tunnel is 16 angstroms long and links the surroundingsolvent with the buried active site. Binding of the CoA moiety in thistunnel positions substrates at the active site, as observed in the C₁₆₄Smutant (described in greater detail below) complexed with malonyl- orhexanoyl-CoA. The conformation of the CoA molecules bound to CHSresembles that observed in other CoA binding enzymes. The adenosinenucleoside is in the 2′-endo conformation with an anti-glycosidic bondtorsion angle. At the tunnel entrance, Lys₅₅, Arg₅₈, and Lys₆₂ hydrogenbond with two phosphates of CoA. Apart from these interactions, and anadditional hydrogen bond between the backbone amide nitrogen of Ala₃₀₈and the first carbonyl of the pantetheine moiety, van der Waals contactsdominate the remaining interactions between CHS and CoA. The pantetheinearm of the CoA extends into the enzyme positioning the terminally boundthioester-linked substrates near Cys₁₆₄.

Both naringenin and resveratrol bind at the active site end of theCoA-binding tunnel. The interactions observed in the naringenin andresveratrol complexes define the coumaroyl-binding and cyclization:pockets. The space to the lower left of the CoA-binding tunnel's endserves as the coumaroyl-binding pocket. Residues of this pocket (Ser₁₃₃,Glu₁₉₂, Thr₁₉₄, Thr₁₉₇, and Ser₃₃₈) surround the coumaroyl-derivedportion of the bound naringenin and resveratrol molecules and interactprimarily through van der Waals contacts. However, the carbonyl oxygenof Gly₂₁₆ hydrogen bonds to the phenolic oxygen of both naringenin andresveratrol and the hydroxyl of Thr₁₉₇ interacts with the carbonyl ofnaringenin derived from coumaroyl-CoA. The identity of the residues inthis pocket likely contributes to the preference for coumaroyl-CoA as asubstrate for parsley CHS over other cinnamoyl-CoA starter molecules,like caffeoyl- or feruloyl-CoA.

In both the naringenin and resveratrol complexes, the malonyl-derivedportion of each molecule occupies a large pocket adjacent to Cys164suggesting this is where the polyketide reaction intermediate cyclizesinto the new ring system and where aromatization of the ring occurs. Thesix-carbon chain of hexanoyl-CoA also binds in this pocket. Physically,the size of the pocket limits the number of acetate additions to three.Phe₂₆₅ separates the coumaroyl-binding site from the cyclization pocketand may function as a mobile steric gate during successive rounds ofpolyketide elongation. Although a polyketide possesses a number ofhydrogen bond acceptors through which specific interactions could aid inproper folding for the cyclization reaction, the residues of thecyclization pocket, including Thr₁₃₂, Met₁₃₇, Phe₂₁₅, Ile₂₅₄, Gly₂₅₆,Phe₂₆₅, and Pro₃₇₅, provide few potential hydrogen bond donors. As inthe coumaroyl-binding pocket, van der Waals contacts dominate theinteraction between CHS and both naringenin and resveratrol. Thus, thesurface topology of the cyclization pocket dictates how themalonyl-derived portion of the polyketide is folded and how thestereochemistry of the cyclization reaction leading to chalconeformation in CHS and resveratrol formation in STS is controlled.

Reaction Mechanism

The position of the CoA thioesters and product analogs in the CHS activesite suggest binding modes for substrates and intermediates in thepolyketide elongation mechanism that are consistent with the knownproduct specificity of CHS. In addition, the stereochemical features ofthe substrate and product analog complexes elucidate the roles ofCys₁₆₄, Phe₂₁₅, His₃₀₃, and Asn₃₃₆ in the reaction mechanism. Utilizingstructural constraints derived from the available complexes, thefollowing reaction sequence is proposed (see FIG. 6).

In the mechanism, binding of p-coumaroyl-CoA initiates the CHS reaction.Functional and structural evidence supports a coumaroyl-first mechanismover a malonyl-first one. Cerulenin, a potent irreversible inhibitor ofCHS, covalently modifies Cys₁₆₄ in CHS (Lanz, et al., J. Biol. Chem.266:9971-9976, 1991). Preincubation of CHS with coumaroyl-CoA preventsinactivation by cerulenin, but pre-incubation with malonyl-CoA does not(Preisig-Mueller, et al., Biochemistry 36:8349-8358, 1997). Also, thelocation of the coumaroyl-derived portion of naringenin and resveratrolin the CHS complexes agrees with a coumaroyl first mechanism, since thepresence of a triketide reaction intermediate attached to Cys₁₆₄ wouldlimit access to the coumaroyl-binding pocket.

After p-coumaroyl-CoA binds to CHS, Cys₁₆₄, activated by His₃₀₃, attacksthe thioester linkage, transferring the coumaroyl moiety to Cys₁₆₄(Monoketide Intermediate). Asn₃₃₆ hydrogen bonds with the carbonyloxygen of the thioester further stabilizing formation of the tetrahedralreaction intermediate. CoA then dissociates from the enzyme, leaving acoumaroyl-thioester at Cys₁₆₄. Binding of the first malonyl-CoApositions the bridging methylene carbon of the malonyl moiety near thecarbonyl carbon of the covalently attached coumaroyl-thioester.Decarboxylation of malonyl-CoA leads to carbanion formation. Resonancebetween the keto and enol species stabilizes the carbanion. Attack ofthis carbanion on the coumaroyl-thioester releases the thiolate anion ofCys₁₆₄ and transfers the coumaroyl group to the acetyl moiety of the CoAthioester (Diketide CoA Thioester). Capture of this elongateddiketide-CoA by Cys₁₆₄ and release of CoA sets the stage for twoadditional rounds of elongation resulting in formation of thetetraketide reaction intermediate.

Asn₃₃₆ appears to play a crucial role in the decarboxylation reaction.Structural evidence shows that the decarboxylation reaction does notrequire transfer of the malonyl moiety to Cys₁₆₄ as originally indicatedby CO₂ exchange assays. Decarboxylation occurs without Cys₁₆₄, since theC₁₆₄S mutant produces acetyl-CoA as determined crystallographically andconfirmed by a functional assay. In the hexanoyl-CoA complex, the sidechain amide of Asn₃₃₆ provides a hydrogen bond to the carbonyl oxygen ofthe thioester. This interaction would stabilize the enolate anionresulting from decarboxylation of malonyl-CoA (see FIG. 6). At the sametime, the lack of formal positive charge at Asn₃₃₆ may preserve thepartial carbanion character of this resonance-stabilized anion, and thusthe nucleophilicity of the carbanion form.

The role of Phe₂₁₅ in the catalytic mechanism is subtler than that ofAsn₃₃₆. Its position in both CoA complexes suggests that it provide vander Waals interactions for substrate binding. However, its conservationin bacterial enzymes related to CHS that do not make flavonoids orstilbenes may indicate a more general catalytic role for Phe₂₁₅. Itsposition near the acetyl moiety of the malonyl-CoA complex suggests thatit participates in decarboxylation by favoring conversion of thenegatively charged carboxyl group to a neutral carbon dioxide molecule.

FIG. 7A depicts the addition of the third malonyl-CoA molecule as athree-dimensional model. The position of the coumaroyl ring in themodeled triketide intermediate is as observed in the naringenin andresveratrol complexes. The coumaroyl-binding pocket locks this moiety inposition, while the acetate units added in subsequent chain extensionsteps bend to fill the cyclization pocket. The backbone of boundhexanoyl-CoA provides a guide for modeling the triketide reactionintermediate attached to Cys₁₆₄. Based on the observed acetyl-CoAcomplex, a rotation of the acetyl group would place the terminalmethylene of the decarboxylated malonyl-CoA in position for nucleophilicattack on the triketide thioester linkage resulting in formation of atetraketide CoA thioester.

The cyclization reaction catalyzed by CHS is an intramolecular Claisencondensation encompassing the three acetate units derived from threemalonyl-CoAs. During cyclization, the nucleophilic methylene groupnearest the coumaroyl moiety attacks the carbonyl carbon of thethioester linked to Cys₁₆₄. Ring closure proceeds through an internalproton transfer from the nucleophilic carbon to the carbonyl oxygen.Modeling of the tetraketide intermediate in a conformation leading tochalcone formation places one of the acidic protons of the nucleophiliccarbon (C6) proximal to the target carbonyl (C1) (see FIG. 7B). Sincethere is no base capable of proton abstraction from the tetraketide, itis proposed that the intermediate itself provides the driving force forcarbanion formation. Protonation of the carbonyl oxygen would alsostabilize the negative charge on the tetrahedral intermediate. Breakdownof this tetrahedral intermediate expels the newly cyclized ring systemfrom Cys₁₆₄. Subsequent aromatization of the trione ring through asecond series of facile internal proton transfers yields chalcone.

Although the cyclization reaction has been modeled as occurring via apolyketide intermediate attached to Cys₁₆₄, it is possible that thereaction proceeds when the polyketide is attached to CoA. The rate ofcyclization versus the rate of reattachment to Cys₁₆₄ would dictatewhich of the two cyclization alternatives is mechanistically preferred.

An important question in the biosynthesis of chalcones concerns theexchangeability of the polyketide reaction intermediates. In thepresence of chalcone reductase (CHR), CHS produces 6-deoxychalcone(Welle & Grisebach, FEBS Lett. 236:22-225, 1988). Mechanistically, CHRmust reduce a ketone on the polyketide intermediate before cyclizationoccurs. Based on the CHS structure, any polyketide attached to Cys₁₆₄would be inaccessible to CHR unless a drastic structural change occursin CHS upon interaction with CHR. While this conformational change ispossible, such a change is difficult to imagine given the buried natureof the CHS active site. This would argue for the presence of moderatelyexchangeable polyketide-CoA reaction intermediates. Consistent with thisidea, a recently identified CHS-like enzyme from Pinus strobus involvedin the biosynthesis of C-methylated chalcones is active only with astarter molecule that is sterically analogous to the diketide-CoAintermediate postulated to be formed after the first condensationreaction in CHS30. These results suggest that the enzymes involved inthe biosynthesis of plant polyketides may require specific localizationin the plant cell to allow efficient channeling of intermediates fromone enzyme to another during the production of particular products.

Cyclization Specificity of CHS and STS

Elucidation of the structure of CHS provided mechanistic insight andactive site configuration for CHS reaction. Homology modeling andsequence alignments suggested evolutionary functional divergence of CHSsuperfamily (type III PKSs) occurs via the preservation of catalyticresidues while using steric variation of other active site residues.Elucidation of the structure of 2-PS confirms the above ‘stericmodulation’ model, by revealing substrate and product specificitydifferences achieved by only three active site mutations, as suggestedby homology model of 2-PS based upon CHS 3D structure.

However, with these structures alone, the structural cause/determinantsof the alternate cyclization seen in the stilbene synthase (STS)subfamily of CHS-like enzymes remained unknown. STS makes the sametetraketide intermediate as CHS, but cyclizes it differently (C2->C7attack instead of C6->C1). STS evolved from CHS independently at leastthree times, with no clear STS consensus sequence.

Elucidation of the structure of pine (Pinus sylvestris) STS according tothe present invention reveals a similar active site configuration, withminor differences. Furthermore, an 18×CHS mutant encompassing observedSTS structural backbone differences proves to have activity and kineticssimilar to STS (see FIG. 18), confirming that observed structuraldifferences between CHS and STS are relevant to mechanistic differences.

It was further determined that ten of the eighteen mutations in 18×CHSprove to be neutral (not related to functional conversion, i.e. analteration in CHS activity), and an 8×CHS mutant with similar STS-likeactivity is made. All of the 8×CHS changes are clustered in a singlearea, although encoded on three different stretches of primary sequence(see FIG. 19). This area is thus implicated as important for STS-likeversus CHS-like cyclization.

Elucidation of the structure of peanut (Arachis hypogaea) STS, as wellas of the 18×CHS engineered STS, show similar three-dimensionalconformational changes in the area implicated by the 8×CHS mutagenicconversion of CHS to STS (see FIG. 20). This implies that a single 3Dsolution to the CHS to STS conversion problem has been found by allthree STS subfamilies, despite variation in primary sequence. Acompensatory increase in bulkiness at CHS residue 98 seems to beinvolved in all three families of STS.

A closer look at where the altered region meets the active site (seeFIG. 22) reveals a consistent change in STS-like enzymes that suggests acyclization switch mechanism (see FIG. 21), involving movement of Thr132to allow a hydrogen-bond chain to transfer an electron from Glu192,through Thr132 and a water (bonded to Ser 338). This electron isproposed to encourage hydrolysis of the tetraketide intermediate off ofthe catalytic cysteine, where decarboxylation of the terminal carboxylgroup drives the STS reaction toward a C2->C7 cyclization. In CHS, thishydrolysis does not occur, and so the C6->C1 cyclization is encouraged,as it serves to break the thioester bond to cysteine.

To test this proposed mechanism, various mutations were made in the18×CHS engineered STS enzyme, in an attempt to revert the productspecificity back to that of CHS, without reversing the other structuralchanges. Single mutations designed to disrupt only the hydrogen-bondingcharacter in the relevant region succeeded in reverting 18CHS's activityfrom STS-like to CHS-like. A few of these mutants produce almost equalamounts of resveratrol and chalcone, which might be useful whenengineered into a plant. This way, the beneficial resveratrol antifungalnatural product could be made, without completely abrogating the vitalCHS-like activity necessary in plants.

The residue implicated as the crucial base for STS-like behavior(Glu192) is not altered in STS. Instead, the adjacent Thr132 changespositions. As a further test of the proposed aldol mechanism, theresidue equivalent to CHS Glu192 was mutated to Gln in both the pine andpeanut STS wild type enzymes. As predicted, both of these single mutantsmade more chalcone and less resveratrol than the wild type STS enzymes.The ratio of products supports the proposed mechanism. The decrease inoverall activity of these mutants is due to the fact that Glu192 is alsoimportant for folding and/or stability, apart from its role incyclization specificity.

Structural Basis for Functionally Novel CHS-like Enzymes

Absolute conservation of Cys₁₆₄, Phe₂₁₅, His₃₀₃, and Asn₃₃₆ occurs inCHS-like sequences, including several bacterial proteins possessing verylow (typically 20-30%) amino acid sequence identity. Moreover, allCHS-like proteins exhibit strong conservation of residues shaping thegeometry of the active site. Although the functions of the bacterialCHS-like proteins remain unknown, these enzymes likely form polyketidesor polyketide-CoA thioesters in a manner resembling CHS. However, stericdifferences resulting from sequence variation in both thecoumaroyl-binding pocket and the cyclization pocket strongly suggestalternate substrate and product specificity in the bacterial enzymes.

The sequence databases include approximately 150 plant enzyme sequencesclassified as CHS like proteins. The substrate and product specificityof a majority of these sequences remains to be determined. In addition,the high sequence similarity of all plant sequences complicatesclassification of these sequences as authentic CHS, STS, ACS, or BBSenzymes. The information provided by the three-dimensional structure ofCHS should make new substrate and product specificity more readilydiscernible from sequence information.

To illustrate the usefulness of structural information in identifyingpotentially new activities, a CHS-related sequence from Gerbera hybrida(GCHS2)32 that is 74% identical with alfalfa CHS2 (SEQ ID NO:1) wasexamined. Modeling the active site architecture of GCHS2 using thestructure of alfalfa CHS2 as a template indicates that GCHS2 will notcatalyze either the CHS-like or STS-like reaction (see FIG. 8). Thisvariation in reaction specificity results from striking stericdifferences in the coumaroyl binding and cyclization pockets thatsubstantially reduce the volume of both pockets from 923 Å³ in CHS to269 Å³ in GCHS2. Side chain variation at positions 197 and 338 (see SEQID NO:1) alter the coumaroyl binding pocket, while the identity ofresidue 256 (see SEQ ID NO:1) dictates major steric changes in thecyclization pocket. The reduced size of these pockets in GCHS2 suggeststhat fewer than three acetate additions will occur, and that a CoAthioester with an acyl moiety smaller than p-coumaroyl initiates thereaction. Recent functional characterization of GCHS2 confirms thisprediction and demonstrates that this enzyme uses acetyl-CoA orbenzoyl-CoA and two condensation reactions with malonyl-CoA to formpyrone products (Eckermann, et al., Nature 396:397-396, 1998).

Crystallization of Additional Polyketide Synthases

Stilbene synthase from Pinus sylvestris (SEQ ID NO:65) was overexpressedin E. coli as an octahistidyl N-terminal fusion protein, purifiedto >90% homogeneity by metal affinity and gel filtration chromatography,and crystallized in the preparation lacking the N-terminal polyhistidinetag (removed by thrombin cleavage) from 13% (w/v) polyethylene glycol(PEG8000), 0.05 M MOPSO, 0.3 M ammonium acetate at pH 7.0. This STS is396 amino acids in length and, like alfalfa CHS (SEQ ID NO:1). exists asa homodimer in solution. The structural coordinates of this pine STS arepresented in Appendix A. STS from Arachis hypogaea (SEQ ID NO:66) wassimilarly expressed and crystallized. The structural coordinates of thispeanut STS are presented in Appendix B.

2-Pyrone synthase (2-PS) from Gerbera hybrida (SEQ ID NO:68) wasexpressed and purified from E. coli in a similar manner to CHS (SEQ IDNO:1) and STS (SEQ ID NO:65). Crystals were obtained from 1.5 M ammoniumsulfate, 011 M Na⁺—succinate, 0.002 MDTTatpH 5.5.

2-Pyrone synthase (2-PS) from Gerbera hybrida (SEQ ID NO:68 forms atriketide from an acetyl-CoA initiator and two acetyl-CoA α-carbanionsderived from decarboxylation of two malonyl-CoAs that cyclizes into the6-methyl-4-hydroxy-2-pyrone. In comparison, alfalfa chalcone synthase 2(SEQ ID NO:1: CHS2; 74% amino acid sequence identity to 2-PS), condensesp-coumaroyl-CoA and three acetyl-CoA α-carbanions derived fromdecarboxylation of three malonyl-CoAs into a tetraketide that cyclizesinto chalcone. A homology model of 2-PS based on the structure of CHS(SEQ ID NO:1) suggested that the 2-PS initiation/elongation cavity issmaller than that of CHS. A smaller cavity would account for theterminal formation of a triketide intermediate prior to cyclization by2-PS.

Expression, Purification and Crystallization of 2-PS.

2-PS was expressed in E. coli, purified and crystallized as describedabove. Gerbera hybrida 2-PS (SEQ ID NO:68) was expressed in E. coliusing the pHIS8 vector and was purified as described for CHS. 2-PScrystals grew at 4° C. in hanging-drops containing a 1:1 mixture of 25mg ml⁻¹ protein and crystallization buffer (1.5 M ammonium sulfate, 50mM succinic acid (pH 5.5), and 5 mM DTT). Before freezing at 105° K,crystals (P3₁21; unit cell dimensions a=82.15 Å, c=241.33 Å; one 2-PSdimer per asymmetric unit) were stepped through stabilizer (50 mMsuccinic acid (pH 5.5), 50 mM ammonium sulfate, and 5 mM DTT) containing5 mM acetoacetyl-CoA and increasing concentrations of glycerol (30%(v/v) final). Diffraction data were collected using a DIP2030 imagingplate system and CuK radiation produced by a rotating anode (wavelength1.54 Å). All images were processed with DENZO/SCALEPACK (Z. Otwinowski,W. Minor, Methods Enzymol. 276:307 (1997)). A total of 179,623reflections were merged to give 60,824 unique reflections (98.2%complete overall to 2.05 Å and 98.1% complete in the highest resolutionshell) with an R_(sym)=0.042 (0.206 in the highest resolution shell) andan α/_of 21.7 (4.5 in the highest resolution shell). The structure of2-PS complexed with acetoacetyl-CoA was determined by molecularreplacement using CHS (SEQ ID NO:1) as a search model and was refined to2.05 Å resolution. The overall fold of 2-PS is the αβαβα motif found inCHS and β-ketoacyl synthase II (KAS II). In addition, the positions ofthe catalytic residues of 2-PS (Cys₁₆₉, His₃₀₈, and Asn₃₄₁; see SEQ IDNO:68), CHS (Cys₁₆₃, His₃₀₃, Asn₃₃₆: see SEQ ID NO:1), and KAS II(Cys₁₆₃, His₃₀₃, and His₃₄₀) are structurally analogous. As expectedfrom sequence homology, the structures of 2-PS and CHS are nearlyidentical and superimpose with a r.m.s. deviation of 0.64 Å for the twoproteins′ α-carbon atoms. Similar to CHS, the 2-PS dimerization surfaceburies 1805 Å² of surface area per monomer and a loop containing acis-peptide bond between Met₁₄₂ and Pro₁₄₃ allows the methionine of onemonomer to protrude into the adjoining monomer's active site. Thus,dimerization allows formation of the complete 2-PS active site.

Acetoacetyl-CoA is a reaction intermediate of 2-PS (SEQ ID NO:68).Electron density for the ligand is well defined in the 2-PS active siteand shows that the acetoacetyl moiety extends from the CoA pantetheinearm into a large internal cavity. The electron density also revealsoxidation of the catalytic cysteine's (Cys₁₆₉) sulfhydryl to sulfinicacid (—SO₂H) (see SEQ ID NO:1). This oxidation state prevents formationof a covalent acetoacetyl-enzyme complex but allows trapping of thebound acetoacetyl-CoA intermediate. Extensive protein-ligand contactsposition CoA at the entrance to the active site and orient theacetoacetyl moiety at the end of a 15 Å long tunnel that opens into acavity that defines the initiation and elongation steps of polyketideformation.

The 2-PS (SEQ ID NO:68) active site cavity consists of twenty-sevenresidues from one monomer and Met142 from the adjoining monomer. Phe₂₂₀and Phe₂₇₀ (see SEQ ID NO:68) mark the boundary between the CoA bindingsite and the initiation/elongation cavity. Near the CoA thioester,Cys₁₆₉, His₃₀₈, and Asn₃₄₁ form the catalytic center of 2-PS (see SEQ IDNO:68). These residues are conserved in all homodimeric iterative PKSs.Based on this, catalytic roles were proposed for each residue that areanalogous to the corresponding residues in CHS. Cys169 (see SEQ IDNO:68) acts as the nucleophile in the reaction and as the attachmentsite for the elongating polyketide chain. Interaction between His₃₀₈ andCys₁₆₉ (see SEQ ID NO:68) maintains the thiolate required forcondensation of the starter molecule. His₃₀₈ and Asn341 (see SEQ IDNO:68) catalyze malonyl-CoA decarboxylation and stabilize the transitionstates during the condensation steps by forming an oxyanion hole thataccommodates the negatively charged tetravalent transition state.Following the first condensation reaction, a diketide remains attachedto Cys₁₆₉ (see SEQ ID NO:68). The second malonyl-CoA then binds,undergoes decarboxylation, and the resulting nucleophilic acetyl-coAα-carbanion performs a second condensation reaction with the enzymebound diketide, ultimately generating the triketide that cyclizes intomethylpyrone.

Comparison of the initiation/elongation cavities of 2-PS (SEQ ID NO:68)and CHS (SEQ ID NO:1) reveal four amino acid differences. In 2-PS,Leu₂₀₂, Met₂₅₉, Leu₂₆₁, and Ile₃₄₃ replace Thr₁₉₇, Ile₂₅₄, Gly₂₅₆, andSer₃₃₈, respectively, of CHS. These four substitutions reduce cavityvolume from 923 Å³ in CHS to 274 Å³ in 2-PS. A model of methylpyrone inthe 2-PS cavity, based on the position of acetoacetyl-CoA, emphasizesthe volume change compared to the CHS-naringenin complex (Accession No.1 CGK, SEQ ID NO:69). Leu₂₀₂ and Ile₃₄₃ occlude the portion of the 2-PScavity corresponding to the coumaroyl-binding site of CHS. Replacementof Gly₂₅₆ in CHS by Leu₂₆₁ in 2-PS severely reduces the size of theactive site cavity. Substitution of Met₂₅₉ in 2-PS for Ile₂₅₄ in CHSproduces a modest alteration in cavity volume. To examine the functionalimportance of these amino acid differences, the initiation/elongationcavity of CHS was altered by mutagenesis to resemble that of 2-PS. Theresulting mutant proteins were screened for activity using eitherp-coumaroyl-CoA or acetyl-CoA as starter molecules. Activities of 2-PS,CHS, and the CHS mutants were determined by monitoring product formationusing a TLC-based radiometric assay. Assay conditions were 100 mM Hepes(pH 7.0), 30 μM starter-CoA (either p-coumaroyl-CoA or acetyl-CoA), and60 μM [¹⁴C]-malonyl-CoA (50,000 cpm) in 100 μl at 25° C. Reactions werequenched with 5% acetic acid, extracted with ethyl acetate, and appliedto TLC plates and developed. Due to the spontaneous cyclization ofchalcone into the flavanone naringenin, activities of CHS are referencedto nanngenin formation.

The x-ray crystal structures of 2-PS (SEQ ID NO:68) and CHS (SEQ IDNO:1) imply that the size of the active site cavity limits polyketidelength and modulates folding of the polyketide chain. Wild-type CHS (SEQID NO:1) generates the tetraketide chalcone and 2-PS produces thetriketide methylpyrone. Likewise, the CHS 1254M mutant (see SEQ ID NO:1)also yields chalcone. Interestingly, the T197L, G256L, and S338I mutants(see SEQ ID NO:1) do not form chalcone. Crystallographic analysis of theG256L and S338I mutants (see SEQ ID NO:1) demonstrates that thesubstituted side-chains adopt conformations similar to the correspondingresidues in 2-PS without altering the position of the protein backbone.Since the T197L, G256L, and S338Imutants (see SEQ ID NO:1) alteredproduct formation, a CHS triple mutant was generated. Consistent withthe proposal that cavity volume dictates polyketide length, theT197L/G256L/S338I mutant (see SEQ ID NO:1) produces only methylpyrone,as confirmed by liquid chromatography/mass spectroscopy (LC/MS).LC/MS/MS analysis was performed by the Mass Spectroscopy facility of theScripps Research Institute. Scaled-up assays (2 ml reaction volume) withthe CHS T197L/G256L/S338I mutant (see SEQ ID NO:1) and 2-PS (SEQ IDNO:68) were performed. Extracts were analyzed on a Hewlett-PackardHP1100 MSD single quadrupole mass spectrometer coupled to a ZorbaxSB-C₁₈ column (5 μm, 2.1 mm×150 mm). HPLC conditions were as follows:gradient system from 0 to 100% methanol in water (each containing 0.2%acetic acid) within 10 mm; flow rate 0.25 ml min⁻¹. LC/MS/MS data fromboth reactions were identical: 6-methyl-4-hydroxy-2-pyrone, R_(t)=5.068mm; [M-H]⁻125; [M-H—CO₂]⁻⁸¹. The numbers show m/z values with relativeintensities in parenthesis. The observed fragmentation matchespreviously published data.

In addition, the size of the cavity in 2-PS (SEQ ID NO:68) and CHS (SEQID NO:1) confers starter molecule specificity. 2-PS accepts acetyl-CoAbut does not use p-coumaroyl-CoA. Structurally, the constricted 2-PSactive site excludes the bulky coumaroyl group. As such, incubation of2-PS in the presence of coumaroyl-CoA and malonyl-CoA yieldsmethylpyrone produced from three malonyl-CoA molecules. In comparison,the larger initiation/elongation cavity of CHS allows for differentsized aliphatic and aromatic starter molecules to be used in vitro withvarying efficiencies. CHS exhibits a 230-fold preference forp-coumaroyl-CoA versus acetyl-CoA. Alterations in the active site cavityof CHS, affect starter molecule preference. The CHS I254M mutant (seeSEQ ID NO:1) is functionally comparable to wild-type enzyme with amodest reduction in specific activity. The T197L and S3381 mutantsexhibit 10-fold and 3-fold preferences, respectively, for coumaroyl-CoA.Moreover, both form a distinct product using coumaroyl-CoA as a startermolecule. In contrast, the G256L mutant favors acetyl-CoA 3-fold. Like2-PS (SEQ ID NO:68), the CHS T197L/G256L/S338I (3×) mutant (see SEQ IDNO:1) only accepts acetyl-CoA (or malonyl-CoA) as the starter molecule.

Functional diversity among other homodimeric iterative PKSs, likep-coumaroyltriacetic acid synthase (CTAS), acridone synthase (ACS), andthe rppA protein from Streptomyces griseus, likely results fromvariations of residues lining the initiation/elongation cavity. Asdemonstrated, positions 197, 256, and 338 (see SEQ ID NO:1) distinguishbetween tetraketide products derived from a final Claisen condensationin wild-type CHS and triketide products derived from an enolate-directedcondensation in the CHS triple mutant. Although CHS, CTAS, and ACSgenerate tetraketides, each enzyme differs in either the cyclizationreaction or in the identity of the starter molecule. CTAS forms the sameenzyme-bound tetraketide as CHS but does not catalyze the finalcyclization reaction. Comparison of these two enzymes reveals thatsubstitution of Thr 197 in CHS (see SEQ ID NO:1) with an asparagine inCTAS may prevent the covalently-bound tetraketide intermediate fromundergoing cyclization into chalcone. ACS uses N-methylanthranoyl-CoA asa starting substrate to produce the alkaloid acridone. Three differencesbetween CHS (Thr₁₃₂, Ser₁₃₃, and Phe₂₆₅; see SEQ ID NO:1) and ACS(Ser₁₃₂, Ala₁₃₃, and Val₂₆₅) may alter starter molecule specificity. InACS, these changes likely widen the portion of the cavity correspondingto the p-coumaroyl-binding site in CHS to accommodateN-methylanthranoyl-CoA binding. Comparative changes in the active sitecavity allow formation of longer polyketides. The rppA protein forms apentaketide from five acetates derived from malonyl-CoA decarboxylation.Thr₁₃₇, Ala₁₃₈, Thr₁₉₉, Leu₂₀₂, Met₂₅₉, Leu₂₆₁, Leu₂₆₈, Pro₃₀₄, andIle₃₄₃ of 2-PS are replaced by Cys₁₀₆, Thr₁₀₇, Cys₁₆₈, Cys₁₇₇, Ile₂₂₈,Tyr₂₃₀, Phe₂₃₇, Ala₂₆₁, and Ala₂₉₅, respectively, in the rppA protein.Models of the rppA protein based on the 2-PS and CHS structures showthat cavity volume is 1145 Å³ in the rppA protein versus 274 Å³ in 2-PS(or 923 Å in CHS). Manipulation of the active site through amino acidsubstitutions offers a strategy for increasing the molecular diversityof polyketide formation through both the choice of starter molecule andthe number of subsequent condensation steps.

The reaction mechanism for polyketide formation and the structural basisfor controlling polyketide length described here may be shared withother more complex iterative (e.g., actinorhodin (act) PKS andtetracenomycin (tcm) PKS) and modular PKSs (e.g., 6-deoxyerythronolide Bsynthase (DEBS)). The structural similarity of the 2-PS, CHS, and KAS IIactive sites, the sequence homology of KAS II and the ketosynthases ofact PKS, tcm PKS, and DEBS, and mutagenesis studies of CHS and act PKSdemonstrating similar roles for the catalytic residues of each proteinindicate that a conserved active site architecture catalyzes similarreactions in these enzymes.

As in 2-PS and CHS, the volume of the active site cavities in other PKSslikely limits the size of the final polyketide. For example, act PKS andtcm PKS generate octaketide and decaketide products, respectively, at asingle active site. This suggests that the active site cavities of thesePKSs differ in size, and are larger than those of 2-PS or CHS.Similarly, the ketosynthases of different DEBS modules accept polyketideintermediates ranging in length from five to twelve carbons. ModularPKSs, like DEBS, use an assembly-line system in which an individualmodule catalyzes one elongation reaction and passes the growingpolyketide to the next module. Although the ketosynthase domains of DEBSare functionally permissive, modulation of active site volume in eachmodule's ketosynthase would provide selectivity for the proper sizedintermediate at each elongation step. Structural differences among PKSsalter the volume of the initiation/elongation cavity to allowdiscrimination between starter molecules and to vary the number ofelongation steps to ultimately direct the nature and length of thepolyketide product.

Functional Conversion of Chalcone Synthase to Stilbene Synthase

All CHS-like enzymes utilize a small number of absolutely conservedcatalytic residues within a single active site to catalyze the iteratiVeaddition of acetate units to a starter molecule. A chalcone synthasereaction sequence starts with initiation, is followed by elongation, andends with cyclization (see FIG. 10). CHS family members differ in theirchoice of starter molecule, number of acetyl additions and cyclizationpathway of the resulting polyketide. Structural and functionalcharacterization of CHS from M. sativa (SEQ ID NO:1) suggested thatsubstrate specificity is modulated in the chalcone synthase superfamilyby steric constraints. Such constraints are provided by a set ofvariable residues lining the active site. Functional conversion throughmutagenesis of alfalfa CHS to a pyrone synthase, and the structuralcharacterization of pyrone synthase (PS) from G. hybrida (daisy) (SEQ IDNO:68) support this model. Thus, homology modeling is a valid approachto gain insight into the specificity's of chalcone synthase superfamilymembers, including members that are identified and/or characterized aswell as those still to be identified and characterized.

Stilbene synthase (STS) is related to CHS, and is thought to have arisenfrom CHS on at least three independent occasions. An amino acid sequencealignment of P. sylvesfris STS (SEQ ID NO:8) and M. sativa CHS (SEQ IDNO:10), along with an evolutionary intermediate, P. sylvestris CHS (SEQID NO:9) shows amino acid sequence homology (FIG. 11). Both CHS and STSform the same linear phenylpropanoid tetraketide intermediate via thesequential condensation of three acetyl units derived fromdecarboxylation of malonyl-CoA with one coumaroyl-CoA starter (FIG. 12).STS forms resveratrol via an intramolecular aldol condensation. Incontrast, CHS utilizes an intramolecular Claisen condensation to producechalcone (FIG. 13).

Function conversion is achieved by mutations of CHS. Mutation of M.sativa (alfalfa) CHS (SEQ ID NO:1) confers wild type STS activityresulting in an STS-like product profile from mutant CHS activity.Specifically, alfalfa wild type CHS activity results in the productionof the plant polyketide synthase product, naringenin, a flavanoneproduct resulting from spontaneous ring closure of chalcone product.Mutant CHS activity results in the production of resveratrol, anexpected product of wild type STS activity, and a decrease in theproduction of naringenin (see FIG. 14).

Based on the structural information, a variety of mutant CHS (SEQ IDNO:1) molecules can be designed. Mutant CHS enzymes can vary withrespect to starter preference, activity, product formation, and thelike. Various CHS mutants as shown in Table 3 above were designed byinvention methods and prepared, and were tested for activity.

Mutant CHS (SEQ ID NO: 1) has altered activity based on assays conductedwith ¹⁴C malonyl-CoA. Products were extracted with ethyl acetate andanalyzed by silica gel thin layer chromatography (TLC) and visualized byautoradiography. Mutants 14B and 2B (Table 3) showed reduced amounts ofnaringenin compared to wild type CHS and little or no resveratrol.Mutants 16B, 4B, 6B, 18× and 22× (Table 3) showed reduced amounts ofnaringenin compared to wild type CHS and various amounts of resveratrol.Mutants 18×CHS (SEQ ID NO:67) and 22×CHS (Table 3) showed the lowestnaringenin amounts and the highest resveratrol amounts, in fact, in 22×the naringenin:resveratrol ratio is similar to that seen with wild typeSTS from P. sylvestris (SEQ ID NO:65).

Specific mutations in 18×CHS (SEQ ID NO:67) by area are as follows, withareas underlined showing residue changes especially important foraltering activity (Appendix C. SEQ ID NO:67): A1: D96A, V98L. V99A,V100M; A2: T131S, S133T, G134T, V135P, M137L; A3: Y157V, M159G, M159V,Y160F, Q165H; A4: L268K, K269G, D270A, G273D.

The 22× mutant consists of 18xCHS (SEQ ID NO:67) plus four additionalmutations in area B1, which flanks A4, and bridges the gap between A1-A3and A4 (see FIG. 16). The 22×CHS has decreased naringenin production(relative to 18×CHS), matching identically the product profile of wildtype STS. These mutations are in an area predicted to be important forcyclization specificity, due to changes seen here in comparing theCHS/resveratrol complex structure to apo and other complexes of CHS.Note that final mutation is only two residues before the first change inA4 region.

Specific mutations in 22×CHS (Table 3) by area are as follows, withareas underlined showing residue changes especially important foraltering activity: A1: D96A, V98L, V99A, V100M; A2: T131S, S133T, G134T,V135P, M137L; A3: Y157V, M158G, M159V, Y160F, Q165H; A4: L268K, K269G,D270A, G273D; B1: D255G, H257K, L258V, H266Q.

The crystal structural coordinates of the 18×CHS mutant (SEQ ID NO:67)are presented in Appendix C. Table 6 shows the relative active sitea-carbon coordinates of the 18×CHS mutant possessing STS-like activity.

TABLE 6 Amino Acid Active Site α- (SEQ ID Carbon Number X Position YPosition Z Position NO: 1) 1 3.754 −8.620 58.411 Thr 132 2 0.541 −10.07559.960 Thr 133 3 0.228 −9.423 49.613 Met 137* 4 0.230 −7.076 55.634 Gln161 5 9.260 −15.931 61.148 Thr 194 6 6.542 −18.097 57.263 Thr 197 713.288 −17.295 51.888 Gly 211 8 15.195 −13.751 60.585 Gly 216 9 6.827−10.404 45.169 Ile 254 10 2.304 −13.379 49.664 Gly 256 11 1.944 −17.21054.954 Leu 263 12 5.520 −16.124 49.059 Phe 265 13 8.197 −14.531 42.889Leu 267 14 11.540 −7.480 56.987 Ser 338 15 8.611 −9.306 62.954 Glu 192*Met 137 from the second monomer

Table 7 shows the wild type CHS (SEQ ID NO:1) active site positions thatdiffer from the coordinates listed in Table 6. The unlisted positionsare equivalent for both CHS-like Claissen and STS-like aldol cyclizationspecificity.

TABLE 7 Amino Acid Active Site α- (SEQ ID Carbon Number X Position YPosition Z Position NO: 1) 1 4.033  −8.884 58.744 Thr 132 2 3.656−11.697 61.297 Ser 133

Table 8 shows various amino acid positions where mutations thereof canenable or enhance STS-like activity in CHS mutants. The α-carbonpositions are those observed in the 18×CHS (SEQ ID NO:67) crystalstructure. The comparison of crystal structure may identify furtherpositions that produce similar results.

TABLE 8 Mutation Enabling α- X Y Z (SEQ ID Location Carbon NumberPosition Position Position NO: 1) Designation 1 2.452 −14.634 67.063V98L A1 2 −0.144 −13.492 69.602 V99A A1 3 2.537 −13.818 72.285 V100M A14 4.117 −6.516 61.579 S131T A2 5 0.541 −10.075 59.960 T133S A2 6 −1.599−9.886 63.127 G134T A2 7 −3.665 −12.840 64.483 V135P A2 8 0.228 −9.42349.613 M137L* A2 9 −1.725 −0.801 63.145 M158G A3 10 −0.401 −5.049 58.793Y160F A3 11 3.525 −11.762 46.471 D255G B1 12 −0.844 −15.289 50.586 H257KB1 13 −2.269 −15.735 54.104 L258V B1 14 5.803 −16.354 45.249 H266Q B1 158.069 −13.510 39.218 L268K A4 16 10.985 −12.040 37.288 K269G A4 1714.223 −10.808 38.865 D270A A4

These results show that a function conversion of CHS to STS can beachieved by designing mutations in the CHS sequence (SEQ ID NO:1) basedon CHS structural information.

Table 9. PDB Accession No. 1EE0. The content of Table 9 is herebyincorporated by reference under 37 C.F.R. § 52(e)(1)(iii) to file“1EE0.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size577,940 bytes.

Table 10. PDB Accession No. 1BI5. The content of Table 10 is herebyincorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file“1BI5.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size619,924 bytes.

Table 11. PDB Accession No. 1D6F. The content of Table 11 is herebyincorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file“1D6F.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size313,654 bytes.

Table 12. PDB Accession No. 1D6I. The content of Table 12 is herebyincorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file“1D6I.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size557,686 bytes.

Table 13. PDB Accession No. 1D6H. The content of Table 13 is herebyincorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file“1D6H.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size302,256 bytes.

Table 14. PDB Accession No. 1BQ6. The content of Table 14 is herebyincorporated by reference under 37 C.F.R. Å 1.52(e)(1)(iii) to file“1BQ6.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size610,166 bytes.

Table 15. PDB Accession No. 1CML. The content of Table 15 is herebyincorporated by reference under 37 C.F.R. Å 1.52(e)(1)(iii) to file“1CML.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size334,974 bytes.

Table 16. PDB Accession No. 1CHW. The content of Table 16 is herebyincorporated by reference under 37 C.F.R. Å 1.52(e)(1)(iii) to file “1CHW.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size592,700 bytes.

Table 17. PDB Accession No. 1CGK. The content of Table 17 is herebyincorporated by reference under 37 C.F.R. Å 1.52(e)(1)(iii) to file “1CGK.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size319,968 bytes.

Table 18. PDB Accession No. 1CGZ. The content of Table 18 is herebyincorporated by reference under 37 C.F.R. Å 1.52(e)(1)(iii) to file“1CGZ.txt” of CD-R disk “S2370-3”, created Mar. 20, 2007, with size318,328 bytes.

Additional References Cited

Schroeder, J. (1999) The Chalcone/Stilbene Synthase-type Family ofCondensing Enzymes in Comprehensive Natural Products Chemistry Barton,D. & Nakanishi, K. (ed.) 1 (Elsevier Science Ltd., Amsterdam 1999).

Ferrer, J.-L., Jez, J. M., Bowman, M. E., Dixon, R. A., and Noel, J. P.(1999) Structure of Chalcone Synthase and the Molecular Basis of PlantPolyketide Biosynthesis. Nature Structural Biology, 6: 775-783.

Jez, J. M., Ferrer, J.-L., Bowman, M. E., Dixon, R. A., and Noel, J. P.(2000) Dissection of malonyl-CoA decarboxylation from polyketideformation in the reaction mechanism of a plant polyketide synthase.Biochemistry, 39: 890-902.

Jez, J. M. & Noel, J. P. (2000) Mechanism of chalcone synthase: pKa ofthe catalytic cysteine and the role of the conserved histidine in aplant polyketide synthase. J. Biol. Chem. 2000 Sep 26 [epub ahead ofprint—in press].

Jez, J. M., Austin, M. B., Ferrer, J.-L., Bowman, M. E., Schroder, J.,and Noel, J. P. (2000) Structural control of polyketide formation inplant-specific polyketide synthases. Chemistry & Biology 7(12):919-930.

Tropf S, Lanz T, Rensing S A, Schroder J, Schroder G Evidence thatstilbene synthases have developed from chalcone synthases several timesin the course of evolution J Mol Evol 1994 June;38(6):610-8.

Suh D Y, Fukuma K, Kagami J, Yamazaki Y, Shibuya M, Ebizuka Y, Sankawa UIdentification of amino acid residues important in the cyclizationreactions of chalcone and stilbene synthases Biochem J 2000 Aug.15;350(Pt 1):229-235.

While the foregoing has been presented with reference to particularembodiments of the invention, it will be appreciated by those skilled inthe art that changes in these embodiments may be made without departingfrom the principles and spirit of the invention, the scope of which isdefined by the appended claims.

APPENDIX A Pinus sylvestris STS ATOM # TYPE RES X Y Z OCC B ATOM 1 CBASP A 5 15.478 −29.459 49.168 1.00 67.43 A ATOM 2 CG ASP A 5 16.008−30.062 47.877 1.00 68.10 A ATOM 3 OD1 ASP A 5 17.184 −30.480 47.8501.00 68.26 A ATOM 4 OD2 ASP A 5 15.247 −30.116 46.890 1.00 68.59 A ATOM5 C ASP A 5 16.056 −27.113 48.532 1.00 65.16 A ATOM 6 O ASP A 5 17.024−26.582 47.995 1.00 64.39 A ATOM 7 N ASP A 5 15.729 −27.703 50.902 1.0067.43 A ATOM 8 CA ASP A 5 16.237 −28.193 49.588 1.00 66.83 A ATOM 9 NPHE A 6 14.800 −26.782 48.261 1.00 64.20 A ATOM 10 CA PHE A 6 14.453−25.779 47.266 1.00 63.13 A ATOM 11 CB PHE A 6 12.938 −25.783 47.0531.00 63.60 A ATOM 12 CG PHE A 6 12.353 −27.157 46.885 1.00 64.51 A ATOM13 CD1 PHE A 6 11.522 −27.695 47.866 1.00 66.17 A ATOM 14 CD2 PHE A 612.642 −27.923 45.760 1.00 63.90 A ATOM 15 CE1 PHE A 6 10.987 −28.97647.729 1.00 65.63 A ATOM 16 CE2 PHE A 6 12.113 −29.206 45.613 1.00 63.56A ATOM 17 CZ PHE A 6 11.285 −29.734 46.598 1.00 64.57 A ATOM 18 C PHE A6 14.926 −24.360 47.606 1.00 62.05 A ATOM 19 O PHE A 6 15.234 −23.57746.707 1.00 61.61 A ATOM 20 N GLU A 7 14.982 −24.029 48.895 1.00 61.34 AATOM 21 CA GLU A 7 15.416 −22.699 49.317 1.00 59.88 A ATOM 22 CB GLU A 715.345 −22.556 50.845 1.00 61.69 A ATOM 23 CG GLU A 7 15.802 −21.18251.365 1.00 63.25 A ATOM 24 CD GLU A 7 15.466 −20.956 52.840 1.00 64.35A ATOM 25 OE1 GLU A 7 14.263 −20.904 53.183 1.00 64.96 A ATOM 26 OE2 GLUA 7 16.401 −20.823 53.661 1.00 64.20 A ATOM 27 C GLU A 7 16.832 −22.42148.838 1.00 57.91 A ATOM 28 O GLU A 7 17.322 −21.298 48.950 1.00 58.52 AATOM 29 N GLY A 8 17.487 −23.455 48.315 1.00 56.11 A ATOM 30 CA GLY A 818.839 −23.312 47.796 1.00 52.75 A ATOM 31 C GLY A 8 18.787 −23.32446.277 1.00 50.24 A ATOM 32 O GLY A 8 19.523 −22.595 45.601 1.00 49.08 AATOM 33 N PHE A 9 17.899 −24.163 45.748 1.00 47.36 A ATOM 34 CA PHE A 917.696 −24.287 44.312 1.00 45.44 A ATOM 35 CB PHE A 9 16.631 −25.34744.028 1.00 46.27 A ATOM 36 CG PHE A 9 16.463 −25.670 42.569 1.00 46.38A ATOM 37 CD1 PHE A 9 17.453 −26.362 41.878 1.00 45.31 A ATOM 38 CD2 PHEA 9 15.308 −25.296 41.889 1.00 46.41 A ATOM 39 CE1 PHE A 9 17.294−26.678 40.532 1.00 46.87 A ATOM 40 CE2 PHE A 9 15.139 −25.608 40.5401.00 46.26 A ATOM 41 CZ PHE A 9 16.131 −26.299 39.862 1.00 46.36 A ATOM42 C PHE A 9 17.219 −22.938 43.779 1.00 43.88 A ATOM 43 O PHE A 9 17.610−22.503 42.695 1.00 42.95 A ATOM 44 N ARG A 10 16.369 −22.285 44.5591.00 42.46 A ATOM 45 CA ARG A 10 15.820 −20.988 44.199 1.00 41.78 A ATOM46 CB ARG A 10 14.759 −20.587 45.227 1.00 42.76 A ATOM 47 CG ARG A 1013.336 −20.513 44.699 1.00 45.24 A ATOM 48 CD ARG A 10 13.108 −19.25343.870 1.00 46.91 A ATOM 49 NE ARG A 10 13.803 −19.267 42.582 1.00 47.12A ATOM 50 CZ ARG A 10 13.848 −18.226 41.753 1.00 47.04 A ATOM 51 NH1 ARGA 10 13.243 −17.092 42.083 1.00 46.16 A ATOM 52 NH2 ARG A 10 14.490−18.316 40.599 1.00 45.13 A ATOM 53 C ARG A 10 16.912 −19.923 44.1451.00 41.81 A ATOM 54 O ARG A 10 17.039 −19.191 43.158 1.00 40.31 A ATOM55 N LYS A 11 17.704 −19.848 45.211 1.00 41.51 A ATOM 56 CA LYS A 1118.771 −18.859 45.306 1.00 42.45 A ATOM 57 CB LYS A 11 19.441 −18.94646.679 1.00 44.35 A ATOM 58 CG LYS A 11 18.520 −18.561 47.831 1.00 47.24A ATOM 59 CD LYS A 11 19.157 −18.828 49.194 1.00 47.39 A ATOM 60 CE LYSA 11 18.222 −18.392 50.321 1.00 48.83 A ATOM 61 NZ LYS A 11 18.760−18.701 51.673 1.00 49.79 A ATOM 62 C LYS A 11 19.819 −18.981 44.2141.00 41.73 A ATOM 63 O LYS A 11 20.409 −17.980 43.801 1.00 41.36 A ATOM64 N LEU A 12 20.048 −20.206 43.749 1.00 41.94 A ATOM 65 CA LEU A 1221.042 −20.465 42.705 1.00 41.33 A ATOM 66 CB LEU A 12 21.631 −21.86942.864 1.00 41.99 A ATOM 67 CG LEU A 12 23.057 −21.952 43.411 1.00 42.59A ATOM 68 CD1 LEU A 12 23.449 −23.403 43.608 1.00 44.32 A ATOM 69 CD2LEU A 12 24.010 −21.276 42.445 1.00 42.25 A ATOM 70 C LEU A 12 20.483−20.321 41.299 1.00 40.77 A ATOM 71 O LEU A 12 21.224 −20.037 40.3571.00 41.09 A ATOM 72 N GLN A 13 19.175 −20.520 41.167 1.00 39.79 A ATOM73 CA GLN A 13 18.490 −20.431 39.884 1.00 38.24 A ATOM 74 CB GLN A 1317.119 −21.113 39.996 1.00 38.10 A ATOM 75 CG GLN A 13 16.185 −20.94338.793 1.00 38.78 A ATOM 76 CD GLN A 13 14.899 −21.761 38.934 1.00 39.17A ATOM 77 OE1 GLN A 13 14.231 −21.723 39.975 1.00 35.94 A ATOM 78 NE2GLN A 13 14.549 −22.500 37.884 1.00 36.91 A ATOM 79 C GLN A 13 18.329−18.996 39.395 1.00 38.22 A ATOM 80 O GLN A 13 18.228 −18.764 38.1951.00 39.15 A ATOM 81 N ARG A 14 18.328 −18.040 40.322 1.00 37.88 A ATOM82 CA ARG A 14 18.149 −16.628 39.990 1.00 37.89 A ATOM 83 CB ARG A 1417.136 −16.013 40.950 1.00 40.76 A ATOM 84 CG ARG A 14 17.583 −16.01242.406 1.00 44.03 A ATOM 85 CD ARG A 14 16.477 −15.471 43.280 1.00 46.98A ATOM 86 NE ARG A 14 16.898 −15.263 44.661 1.00 49.61 A ATOM 87 CZ ARGA 14 16.112 −14.748 45.600 1.00 50.12 A ATOM 88 NH1 ARG A 14 14.868−14.394 45.298 1.00 51.87 A ATOM 89 NH2 ARG A 14 16.567 −14.577 46.8331.00 49.78 A ATOM 90 C ARG A 14 19.431 −15.796 40.010 1.00 37.27 A ATOM91 O ARG A 14 20.383 −16.128 40.708 1.00 37.71 A ATOM 92 N ALA A 1519.434 −14.702 39.250 1.00 36.59 A ATOM 93 CA ALA A 15 20.592 −13.81139.144 1.00 36.04 A ATOM 94 CB ALA A 15 20.561 −13.083 37.805 1.00 35.74A ATOM 95 C ALA A 15 20.675 −12.797 40.285 1.00 36.64 A ATOM 96 O ALA A15 19.668 −12.470 40.906 1.00 36.28 A ATOM 97 N ASP A 16 21.877 −12.28440.540 1.00 36.70 A ATOM 98 CA ASP A 16 22.093 −11.331 41.626 1.00 37.04A ATOM 99 CB ASP A 16 23.517 −11.467 42.181 1.00 37.71 A ATOM 100 CG ASPA 16 23.864 −12.885 42.578 1.00 39.12 A ATOM 101 OD1 ASP A 16 23.005−13.579 43.161 1.00 41.62 A ATOM 102 OD2 ASP A 16 25.010 −13.301 42.3191.00 39.23 A ATOM 103 C ASP A 16 21.871 −9.857 41.292 1.00 37.37 A ATOM104 O ASP A 16 21.127 −9.152 41.978 1.00 38.64 A ATOM 105 N GLY A 1722.523 −9.387 40.240 1.00 35.60 A ATOM 106 CA GLY A 17 22.422 −7.98439.903 1.00 35.63 A ATOM 107 C GLY A 17 21.159 −7.453 39.272 1.00 35.92A ATOM 108 O GLY A 17 20.077 −8.023 39.380 1.00 35.96 A ATOM 109 N PHE A18 21.329 −6.318 38.607 1.00 36.31 A ATOM 110 CA PHE A 18 20.253 −5.63637.923 1.00 34.75 A ATOM 111 CB PHE A 18 20.466 −4.126 38.012 1.00 37.21A ATOM 112 CG PHE A 18 19.578 −3.441 39.004 1.00 39.74 A ATOM 113 CD1PHE A 18 20.048 −2.351 39.732 1.00 39.87 A ATOM 114 CD2 PHE A 18 18.262−3.862 39.195 1.00 40.31 A ATOM 115 CE1 PHE A 18 19.223 −1.690 40.6371.00 40.82 A ATOM 116 CE2 PHE A 18 17.426 −3.204 40.101 1.00 40.34 AATOM 117 CZ PHE A 18 17.910 −2.119 40.823 1.00 41.49 A ATOM 118 C PHE A18 20.257 −6.048 36.469 1.00 33.11 A ATOM 119 O PHE A 18 21.321 −6.25135.886 1.00 30.89 A ATOM 120 N ALA A 19 19.066 −6.184 35.895 1.00 32.19A ATOM 121 CA ALA A 19 18.932 −6.528 34.488 1.00 32.21 A ATOM 122 CB ALAA 19 17.458 −6.639 34.106 1.00 32.97 A ATOM 123 C ALA A 19 19.593 −5.36233.746 1.00 32.44 A ATOM 124 O ALA A 19 19.319 −4.187 34.039 1.00 30.18A ATOM 125 N SER A 20 20.464 −5.673 32.792 1.00 30.51 A ATOM 126 CA SERA 20 21.158 −4.611 32.095 1.00 29.55 A ATOM 127 CB SER A 20 22.575−4.502 32.646 1.00 29.41 A ATOM 128 OG SER A 20 22.544 −4.494 34.0621.00 31.94 A ATOM 129 C SER A 20 21.210 −4.779 30.598 1.00 29.71 A ATOM130 O SER A 20 21.222 −5.897 30.083 1.00 31.07 A ATOM 131 N ILE A 2121.231 −3.651 29.900 1.00 28.89 A ATOM 132 CA ILE A 21 21.324 −3.65128.454 1.00 29.32 A ATOM 133 CB ILE A 21 20.827 −2.328 27.862 1.00 29.06A ATOM 134 CG2 ILE A 21 20.864 −2.401 26.358 1.00 29.04 A ATOM 135 CG1ILE A 21 19.403 −2.033 28.344 1.00 30.26 A ATOM 136 CD1 ILE A 21 18.400−3.115 28.026 1.00 33.08 A ATOM 137 C ILE A 21 22.817 −3.802 28.185 1.0030.88 A ATOM 138 O ILE A 21 23.619 −2.964 28.602 1.00 30.81 A ATOM 139 NLEU A 22 23.194 −4.872 27.500 1.00 30.73 A ATOM 140 CA LEU A 22 24.600−5.121 27.240 1.00 29.37 A ATOM 141 CB LEU A 22 24.926 −6.563 27.6061.00 27.95 A ATOM 142 CG LEU A 22 24.496 −6.947 29.019 1.00 26.37 A ATOM143 CD1 LEU A 22 24.854 −8.404 29.301 1.00 26.97 A ATOM 144 CD2 LEU A 2225.178 −6.019 30.006 1.00 27.73 A ATOM 145 C LEU A 22 25.000 −4.84325.801 1.00 30.57 A ATOM 146 O LEU A 22 26.190 −4.902 25.457 1.00 30.82A ATOM 147 N ALA A 23 24.007 −4.537 24.966 1.00 29.20 A ATOM 148 CA ALAA 23 24.255 −4.240 23.556 1.00 27.79 A ATOM 149 CB ALA A 23 24.867−5.449 22.865 1.00 24.35 A ATOM 150 C ALA A 23 22.989 −3.804 22.825 1.0027.34 A ATOM 151 O ALA A 23 21.877 −4.233 23.150 1.00 25.25 A ATOM 152 NILE A 24 23.169 −2.934 21.837 1.00 27.98 A ATOM 153 CA ILE A 24 22.048−2.444 21.054 1.00 27.20 A ATOM 154 CB ILE A 24 21.643 −1.002 21.4441.00 26.17 A ATOM 155 CG2 ILE A 24 20.398 −.596 20.665 1.00 26.40 A ATOM156 CG1 ILE A 24 21.361 −.895 22.945 1.00 26.96 A ATOM 157 CD1 ILE A 2420.943 .540 23.399 1.00 22.86 A ATOM 158 C ILE A 24 22.409 −2.437 19.5721.00 27.82 A ATOM 159 O ILE A 24 23.418 −1.859 19.165 1.00 27.57 A ATOM160 N GLY A 25 21.568 −3.098 18.782 1.00 28.16 A ATOM 161 CA GLY A 2521.746 −3.166 17.347 1.00 26.42 A ATOM 162 C GLY A 25 20.512 −2.56316.685 1.00 28.50 A ATOM 163 O GLY A 25 19.409 −2.612 17.241 1.00 26.10A ATOM 164 N THR A 26 20.699 −2.012 15.490 1.00 28.50 A ATOM 165 CA THRA 26 19.621 −1.377 14.741 1.00 30.82 A ATOM 166 CB THR A 26 19.708 .16814.908 1.00 32.46 A ATOM 167 OG1 THR A 26 18.878 .576 16.003 1.00 32.28A ATOM 168 CG2 THR A 26 19.302 .894 13.629 1.00 34.07 A ATOM 169 C THR A26 19.691 −1.746 13.258 1.00 30.38 A ATOM 170 O THR A 26 20.776 −1.87012.694 1.00 30.95 A ATOM 171 N ALA A 27 18.533 −1.914 12.630 1.00 28.84A ATOM 172 CA ALA A 27 18.495 −2.263 11.220 1.00 27.36 A ATOM 173 CB ALAA 27 18.361 −3.753 11.075 1.00 26.92 A ATOM 174 C ALA A 27 17.346 −1.56410.506 1.00 26.05 A ATOM 175 O ALA A 27 16.306 −1.337 11.089 1.00 23.77A ATOM 176 N ASN A 28 17.536 −1.231 9.235 1.00 28.03 A ATOM 177 CA ASN A28 16.490 −.573 8.457 1.00 28.64 A ATOM 178 CB ASN A 28 16.646 .9488.528 1.00 27.80 A ATOM 179 CG ASN A 28 16.309 1.503 9.893 1.00 29.20 AATOM 180 OD1 ASN A 28 17.197 1.766 10.715 1.00 28.54 A ATOM 181 ND2 ASNA 28 15.013 1.675 10.152 1.00 26.02 A ATOM 182 C ASN A 28 16.481 −1.0016.989 1.00 28.59 A ATOM 183 O ASN A 28 17.525 −1.282 6.420 1.00 28.02 AATOM 184 N PRO A 29 15.292 −1.034 6.356 1.00 29.65 A ATOM 185 CD PRO A29 13.967 −.696 6.908 1.00 28.87 A ATOM 186 CA PRO A 29 15.179 −1.4254.947 1.00 29.12 A ATOM 187 CB PRO A 29 13.671 −1.388 4.686 1.00 30.72 AATOM 188 CG PRO A 29 13.061 −1.530 6.048 1.00 32.13 A ATOM 189 C PRO A29 15.932 −.409 4.083 1.00 31.07 A ATOM 190 O PRO A 29 16.037 .768 4.4441.00 29.67 A ATOM 191 N PRO A 30 16.452 −.853 2.927 1.00 32.61 A ATOM192 CD PRO A 30 16.229 −2.205 2.388 1.00 33.12 A ATOM 193 CA PRO A 3017.210 −.045 1.966 1.00 33.75 A ATOM 194 CB PRO A 30 17.300 −.956 .7481.00 33.69 A ATOM 195 CG PRO A 30 17.308 −2.305 1.351 1.00 34.85 A ATOM196 C PRO A 30 16.553 1.276 1.618 1.00 34.72 A ATOM 197 O PRO A 3017.123 2.352 1.826 1.00 33.78 A ATOM 198 N ASN A 31 15.342 1.172 1.0841.00 36.47 A ATOM 199 CA ASN A 31 14.577 2.332 .656 1.00 35.87 A ATOM200 CB ASN A 31 13.179 1.898 .222 1.00 37.58 A ATOM 201 CG ASN A 3112.379 3.033 −.377 1.00 38.77 A ATOM 202 OD1 ASN A 31 12.852 3.738−1.267 1.00 42.91 A ATOM 203 ND2 ASN A 31 11.158 3.208 .097 1.00 38.97 AATOM 204 C ASN A 31 14.466 3.444 1.682 1.00 36.12 A ATOM 205 O ASN A 3113.752 3.330 2.678 1.00 35.66 A ATOM 206 N ALA A 32 15.190 4.526 1.4311.00 35.45 A ATOM 207 CA ALA A 32 15.139 5.680 2.300 1.00 35.87 A ATOM208 CB ALA A 32 16.501 6.300 2.428 1.00 34.90 A ATOM 209 C ALA A 3214.186 6.633 1.603 1.00 36.32 A ATOM 210 O ALA A 32 14.450 7.062 .4811.00 36.89 A ATOM 211 N VAL A 33 13.066 6.935 2.254 1.00 37.11 A ATOM212 CA VAL A 33 12.072 7.838 1.687 1.00 38.65 A ATOM 213 CB VAL A 3310.628 7.294 1.858 1.00 39.24 A ATOM 214 CG1 VAL A 33 10.507 5.921 1.2481.00 38.32 A ATOM 215 CG2 VAL A 33 10.255 7.256 3.337 1.00 39.28 A ATOM216 C VAL A 33 12.135 9.195 2.371 1.00 40.05 A ATOM 217 O VAL A 3312.190 9.281 3.597 1.00 40.74 A ATOM 218 N ASP A 34 12.120 10.259 1.5791.00 41.52 A ATOM 219 CA ASP A 34 12.159 11.601 2.140 1.00 42.79 A ATOM220 CB ASP A 34 12.984 12.526 1.239 1.00 45.56 A ATOM 221 CG ASP A 3414.476 12.234 1.316 1.00 47.51 A ATOM 222 OD1 ASP A 34 15.219 12.722.439 1.00 49.63 A ATOM 223 OD2 ASP A 34 14.905 11.524 2.258 1.00 48.98 AATOM 224 C ASP A 34 10.735 12.120 2.287 1.00 42.33 A ATOM 225 O ASP A 349.951 12.093 1.338 1.00 42.08 A ATOM 226 N GLN A 35 10.407 12.582 3.4901.00 41.73 A ATOM 227 CA GLN A 35 9.076 13.098 3.787 1.00 41.81 A ATOM228 CB GLN A 35 9.020 13.584 5.243 1.00 40.69 A ATOM 229 CG GLN A 357.627 13.923 5.764 1.00 40.17 A ATOM 230 CD GLN A 35 6.798 12.688 6.0671.00 40.34 A ATOM 231 OE1 GLN A 35 6.692 11.785 5.244 1.00 39.84 A ATOM232 NE2 GLN A 35 6.200 12.649 7.252 1.00 39.72 A ATOM 233 C GLN A 358.686 14.241 2.843 1.00 42.93 A ATOM 234 O GLN A 35 7.504 14.483 2.6131.00 44.31 A ATOM 235 N SER A 36 9.677 14.940 2.294 1.00 43.00 A ATOM236 CA SER A 36 9.404 16.056 1.391 1.00 42.43 A ATOM 237 CB SER A 3610.701 16.798 1.060 1.00 42.98 A ATOM 238 OG SER A 36 11.126 17.5822.162 1.00 44.09 A ATOM 239 C SER A 36 8.705 15.666 .092 1.00 41.13 AATOM 240 O SER A 36 7.772 16.339 −.345 1.00 39.36 A ATOM 241 N THR A 379.155 14.579 −.522 1.00 39.75 A ATOM 242 CA THR A 37 8.575 14.134 −1.7831.00 39.31 A ATOM 243 CB THR A 37 9.686 13.652 −2.762 1.00 39.54 A ATOM244 OG1 THR A 37 10.694 14.666 −2.877 1.00 39.51 A ATOM 245 CG2 THR A 379.107 13.383 −4.151 1.00 40.15 A ATOM 246 C THR A 37 7.557 13.010 −1.5901.00 38.36 A ATOM 247 O THR A 37 7.066 12.434 −2.564 1.00 38.53 A ATOM248 N TYR A 38 7.225 12.697 −.342 1.00 36.06 A ATOM 249 CA TYR A 386.274 11.625 −.124 1.00 36.72 A ATOM 250 CB TYR A 38 6.232 11.187 1.3351.00 35.69 A ATOM 251 CG TYR A 38 5.647 9.801 1.479 1.00 35.07 A ATOM252 CD1 TYR A 38 6.260 8.704 .873 1.00 35.39 A ATOM 253 CE1 TYR A 385.724 7.420 .983 1.00 34.19 A ATOM 254 CD2 TYR A 38 4.476 9.585 2.2011.00 35.84 A ATOM 255 CE2 TYR A 38 3.930 8.308 2.320 1.00 34.78 A ATOM256 CZ TYR A 38 4.561 7.229 1.710 1.00 33.22 A ATOM 257 OH TYR A 384.037 5.967 1.840 1.00 30.24 A ATOM 258 C TYR A 38 4.875 12.002 −.5721.00 37.11 A ATOM 259 O TYR A 38 4.125 11.151 −1.057 1.00 36.68 A ATOM260 N PRO A 39 4.495 13.279 −.407 1.00 36.61 A ATOM 261 CD PRO A 395.087 14.349 .413 1.00 35.84 A ATOM 262 CA PRO A 39 3.151 13.648 −.8411.00 36.96 A ATOM 263 CB PRO A 39 3.068 15.118 −.459 1.00 37.53 A ATOM264 CG PRO A 39 3.869 15.155 .811 1.00 37.43 A ATOM 265 C PRO A 39 2.91713.399 −2.330 1.00 36.68 A ATOM 266 O PRO A 39 1.939 12.749 −2.700 1.0037.75 A ATOM 267 N ASP A 40 3.803 13.901 −3.187 1.00 35.67 A ATOM 268 CAASP A 40 3.626 13.681 −4.617 1.00 37.12 A ATOM 269 CB ASP A 40 4.71414.387 −5.438 1.00 38.06 A ATOM 270 CG ASP A 40 4.556 15.905 −5.457 1.0041.46 A ATOM 271 OD1 ASP A 40 3.426 16.411 −5.246 1.00 41.34 A ATOM 272OD2 ASP A 40 5.570 16.595 −5.709 1.00 43.90 A ATOM 273 C ASP A 40 3.66312.187 −4.913 1.00 36.95 A ATOM 274 O ASP A 40 2.752 11.654 −5.547 1.0038.21 A ATOM 275 N PHE A 41 4.715 11.521 −4.439 1.00 35.19 A ATOM 276 CAPHE A 41 4.907 10.090 −4.637 1.00 35.05 A ATOM 277 CB PHE A 41 6.2369.647 −4.021 1.00 35.93 A ATOM 278 CG PHE A 41 6.379 8.155 −3.916 1.0034.85 A ATOM 279 CD1 PHE A 41 6.487 7.375 −5.051 1.00 36.28 A ATOM 280CD2 PHE A 41 6.354 7.527 −2.681 1.00 36.32 A ATOM 281 CE1 PHE A 41 6.5665.982 −4.960 1.00 36.91 A ATOM 282 CE2 PHE A 41 6.431 6.138 −2.579 1.0035.53 A ATOM 283 CZ PHE A 41 6.536 5.365 −3.724 1.00 35.23 A ATOM 284 CPHE A 41 3.792 9.203 −4.071 1.00 34.73 A ATOM 285 O PHE A 41 3.370 8.253−4.724 1.00 32.31 A ATOM 286 N TYR A 42 3.347 9.501 −2.848 1.00 35.03 AATOM 287 CA TYR A 42 2.283 8.734 −2.189 1.00 36.12 A ATOM 288 CB TYR A42 2.042 9.251 −.761 1.00 37.39 A ATOM 289 CG TYR A 42 .882 8.580 −.0411.00 39.07 A ATOM 290 CD1 TYR A 42 .912 7.220 .270 1.00 38.88 A ATOM 291CE1 TYR A 42 −.164 6.599 .908 1.00 40.03 A ATOM 292 CD2 TYR A 42 −.2569.306 .311 1.00 41.58 A ATOM 293 CE2 TYR A 42 −1.339 8.695 .950 1.0042.57 A ATOM 294 CZ TYR A 42 −1.286 7.340 1.242 1.00 42.03 A ATOM 295 OHTYR A 42 −2.371 6.730 1.837 1.00 42.82 A ATOM 296 C TYR A 42 .972 8.797−2.966 1.00 35.76 A ATOM 297 O TYR A 42 .263 7.794 −3.067 1.00 35.92 AATOM 298 N PHE A 43 .657 9.973 −3.511 1.00 35.17 A ATOM 299 CA PHE A 43−.570 10.157 −4.275 1.00 35.00 A ATOM 300 CB PHE A 43 −1.008 11.621−4.227 1.00 34.32 A ATOM 301 CG PHE A 43 −1.821 11.946 −3.019 1.00 35.42A ATOM 302 CD1 PHE A 43 −1.258 11.874 −1.749 1.00 36.46 A ATOM 303 CD2PHE A 43 −3.182 12.209 −3.131 1.00 36.17 A ATOM 304 CE1 PHE A 43 −2.04312.050 −.605 1.00 36.76 A ATOM 305 CE2 PHE A 43 −3.973 12.385 −1.9951.00 36.73 A ATOM 306 CZ PHE A 43 −3.402 12.303 −.733 1.00 36.01 A ATOM307 C PHE A 43 −.466 9.674 −5.711 1.00 34.97 A ATOM 308 O PHE A 43−1.464 9.296 −6.324 1.00 35.50 A ATOM 309 N ARG A 44 .749 9.670 −6.2381.00 35.11 A ATOM 310 CA ARG A 44 .978 9.213 −7.594 1.00 36.10 A ATOM311 CB ARG A 44 2.377 9.628 −8.067 1.00 35.40 A ATOM 312 CG ARG A 442.664 9.344 −9.535 1.00 35.13 A ATOM 313 CD ARG A 44 4.163 9.339 −9.8111.00 35.91 A ATOM 314 NE ARG A 44 4.677 7.973 −9.832 1.00 37.90 A ATOM315 CZ ARG A 44 5.852 7.593 −9.347 1.00 36.82 A ATOM 316 NH1 ARG A 446.669 8.472 −8.787 1.00 35.87 A ATOM 317 NH2 ARG A 44 6.203 6.319 −9.4201.00 35.52 A ATOM 318 C ARG A 44 .875 7.692 −7.596 1.00 36.32 A ATOM 319O ARG A 44 .045 7.116 −8.289 1.00 37.41 A ATOM 320 N ILE A 45 1.7247.051 −6.801 1.00 36.73 A ATOM 321 CA ILE A 45 1.761 5.597 −6.709 1.0036.73 A ATOM 322 CB ILE A 45 2.832 5.150 −5.657 1.00 37.01 A ATOM 323CG2 ILE A 45 2.165 4.717 −4.354 1.00 36.42 A ATOM 324 CG1 ILE A 45 3.7054.028 −6.238 1.00 36.57 A ATOM 325 CD1 ILE A 45 2.967 2.746 −6.571 1.0038.47 A ATOM 326 C ILE A 45 .391 4.990 −6.379 1.00 36.30 A ATOM 327 OILE A 45 .153 3.810 −6.621 1.00 34.20 A ATOM 328 N THR A 46 −.515 5.801−5.838 1.00 38.01 A ATOM 329 CA THR A 46 −1.850 5.310 −5.493 1.00 37.39A ATOM 330 CB THR A 46 −2.252 5.740 −4.074 1.00 36.17 A ATOM 331 OG1 THRA 46 −1.982 7.136 −3.893 1.00 33.06 A ATOM 332 CG2 THR A 46 −1.479 4.926−3.048 1.00 37.56 A ATOM 333 C THR A 46 −2.958 5.728 −6.457 1.00 38.51 AATOM 334 O THR A 46 −4.132 5.436 −6.219 1.00 37.81 A ATOM 335 N GLY A 47−2.584 6.408 −7.540 1.00 39.96 A ATOM 336 CA GLY A 47 −3.565 6.846−8.521 1.00 42.56 A ATOM 337 C GLY A 47 −4.502 7.909 −7.984 1.00 44.81 AATOM 338 O GLY A 47 −5.650 8.022 −8.420 1.00 43.82 A ATOM 339 N ASN A 48−4.005 8.694 −7.035 1.00 46.78 A ATOM 340 CA ASN A 48 −4.797 9.746−6.421 1.00 49.83 A ATOM 341 CB ASN A 48 −4.906 9.495 −4.911 1.00 49.33A ATOM 342 CG ASN A 48 −5.900 8.388 −4.562 1.00 49.27 A ATOM 343 OD1 ASNA 48 −7.092 8.641 −4.364 1.00 47.01 A ATOM 344 ND2 ASN A 48 −5.410 7.156−4.494 1.00 47.58 A ATOM 345 C ASN A 48 −4.222 11.141 −6.674 1.00 52.04A ATOM 346 O ASN A 48 −4.160 11.965 −5.765 1.00 51.94 A ATOM 347 N GLU A49 −3.800 11.407 −7.906 1.00 54.73 A ATOM 348 CA GLU A 49 −3.246 12.720−8.234 1.00 57.69 A ATOM 349 CB GLU A 49 −2.369 12.637 −9.485 1.00 59.73A ATOM 350 CG GLU A 49 −.879 12.518 −9.183 1.00 63.54 A ATOM 351 CD GLUA 49 −.007 12.726 −10.417 1.00 66.25 A ATOM 352 OE1 GLU A 49 −.28213.681 −11.186 1.00 65.49 A ATOM 353 OE2 GLU A 49 .959 11.945 −10.6051.00 66.00 A ATOM 354 C GLU A 49 −4.329 13.776 −8.446 1.00 58.31 A ATOM355 O GLU A 49 −4.185 14.927 −8.035 1.00 59.07 A ATOM 356 N HIS A 50−5.418 13.371 −9.084 1.00 58.62 A ATOM 357 CA HIS A 50 −6.527 14.268−9.374 1.00 59.61 A ATOM 358 CB HIS A 50 −7.610 13.497 −10.121 1.0060.54 A ATOM 359 CG HIS A 50 −8.106 12.301 −9.376 1.00 61.50 A ATOM 360CD2 HIS A 50 −7.982 10.977 −9.629 1.00 62.11 A ATOM 361 ND1 HIS A 50−8.800 12.402 −8.190 1.00 62.16 A ATOM 362 CE1 HIS A 50 −9.084 11.191−7.744 1.00 62.79 A ATOM 363 NE2 HIS A 50 −8.599 10.309 −8.599 1.0062.52 A ATOM 364 C HIS A 50 −7.149 14.957 −8.153 1.00 59.88 A ATOM 365 OHIS A 50 −7.651 16.080 −8.270 1.00 60.59 A ATOM 366 N ASN A 51 −7.12814.296 −6.995 1.00 58.82 A ATOM 367 CA ASN A 51 −7.719 14.870 −5.7811.00 56.81 A ATOM 368 CB ASN A 51 −8.203 13.767 −4.843 1.00 56.29 A ATOM369 CG ASN A 51 −9.152 14.286 −3.790 1.00 56.26 A ATOM 370 OD1 ASN A 51−8.874 15.284 −3.123 1.00 56.98 A ATOM 371 ND2 ASN A 51 −10.282 13.614−3.632 1.00 56.27 A ATOM 372 C ASN A 51 −6.760 15.785 −5.028 1.00 56.35A ATOM 373 O ASN A 51 −6.394 15.529 −3.877 1.00 55.87 A ATOM 374 N THR A52 −6.376 16.860 −5.705 1.00 55.80 A ATOM 375 CA THR A 52 −5.463 17.865−5.188 1.00 54.81 A ATOM 376 CB THR A 52 −5.459 19.087 −6.111 1.00 55.61A ATOM 377 OG1 THR A 52 −6.814 19.464 −6.398 1.00 54.96 A ATOM 378 CG2THR A 52 −4.736 18.764 −7.417 1.00 55.96 A ATOM 379 C THR A 52 −5.75018.336 −3.767 1.00 53.99 A ATOM 380 O THR A 52 −4.838 18.786 −3.071 1.0053.61 A ATOM 381 N GLU A 53 −7.007 18.241 −3.339 1.00 53.25 A ATOM 382CA GLU A 53 −7.384 18.670 −1.991 1.00 52.66 A ATOM 383 CB GLU A 53−8.908 18.712 −1.848 1.00 53.87 A ATOM 384 CG GLU A 53 −9.545 19.936−2.469 1.00 56.65 A ATOM 385 CD GLU A 53 −9.077 21.226 −1.809 1.00 58.56A ATOM 386 OE1 GLU A 53 −9.448 21.471 −.638 1.00 59.21 A ATOM 387 OE2GLU A 53 −8.331 21.990 −2.460 1.00 59.26 A ATOM 388 C GLU A 53 −6.79517.774 −.902 1.00 51.50 A ATOM 389 O GLU A 53 −6.097 18.248 −.001 1.0050.48 A ATOM 390 N LEU A 54 −7.084 16.479 −.986 1.00 50.21 A ATOM 391 CALEU A 54 −6.580 15.524 −.006 1.00 49.09 A ATOM 392 CB LEU A 54 −7.09814.123 −.324 1.00 46.64 A ATOM 393 CG LEU A 54 −6.867 13.107 .787 1.0045.40 A ATOM 394 CD1 LEU A 54 −7.488 13.628 2.071 1.00 43.87 A ATOM 395CD2 LEU A 54 −7.464 11.766 .393 1.00 44.37 A ATOM 396 C LEU A 54 −5.05715.524 −.019 1.00 49.00 A ATOM 397 O LEU A 54 −4.411 15.498 1.033 1.0047.49 A ATOM 398 N LYS A 55 −4.497 15.556 −1.226 1.00 48.68 A ATOM 399CA LYS A 55 −3.055 15.572 −1.408 1.00 47.72 A ATOM 400 CB LYS A 55−2.729 15.647 −2.901 1.00 48.44 A ATOM 401 CG LYS A 55 −1.262 15.406−3.270 1.00 50.21 A ATOM 402 CD LYS A 55 −1.057 15.477 −4.794 1.00 50.11A ATOM 403 CE LYS A 55 .398 15.232 −5.188 1.00 51.15 A ATOM 404 NZ LYS A55 .637 15.423 −6.646 1.00 51.72 A ATOM 405 C LYS A 55 −2.465 16.773−.667 1.00 46.95 A ATOM 406 O LYS A 55 −1.555 16.624 .148 1.00 45.99 AATOM 407 N ASP A 56 −2.993 17.962 −.938 1.00 47.40 A ATOM 408 CA ASP A56 −2.487 19.158 −.277 1.00 48.44 A ATOM 409 CB ASP A 56 −3.171 20.423−.811 1.00 50.05 A ATOM 410 CG ASP A 56 −2.567 21.706 −.233 1.00 52.26 AATOM 411 OD1 ASP A 56 −1.327 21.769 −.059 1.00 52.72 A ATOM 412 OD2 ASPA 56 −3.332 22.656 .038 1.00 53.74 A ATOM 413 C ASP A 56 −2.716 19.0271.217 1.00 47.51 A ATOM 414 O ASP A 56 −1.932 19.538 2.026 1.00 47.63 AATOM 415 N LYS A 57 −3.793 18.337 1.582 1.00 46.00 A ATOM 416 CA LYS A57 −4.098 18.115 2.988 1.00 45.09 A ATOM 417 CB LYS A 57 −5.500 17.5253.150 1.00 46.26 A ATOM 418 CG LYS A 57 −5.753 16.920 4.524 1.00 47.34 AATOM 419 CD LYS A 57 −7.006 17.481 5.180 1.00 48.29 A ATOM 420 CE LYS A57 −8.282 17.064 4.462 1.00 46.87 A ATOM 421 NZ LYS A 57 −9.480 17.6275.149 1.00 46.62 A ATOM 422 C LYS A 57 −3.068 17.164 3.593 1.00 42.98 AATOM 423 O LYS A 57 −2.712 17.280 4.762 1.00 41.90 A ATOM 424 N PHE A 58−2.587 16.229 2.786 1.00 41.09 A ATOM 425 CA PHE A 58 −1.606 15.2703.261 1.00 40.95 A ATOM 426 CB PHE A 58 −1.620 14.033 2.371 1.00 40.96 AATOM 427 CG PHE A 58 −.646 12.975 2.786 1.00 42.12 A ATOM 428 CD1 PHE A58 .574 12.838 2.128 1.00 42.03 A ATOM 429 CD2 PHE A 58 −.957 12.0933.815 1.00 41.57 A ATOM 430 CE1 PHE A 58 1.470 11.834 2.484 1.00 42.26 AATOM 431 CE2 PHE A 58 −.064 11.085 4.181 1.00 42.43 A ATOM 432 CZ PHE A58 1.150 10.955 3.512 1.00 40.79 A ATOM 433 C PHE A 58 −.219 15.8883.300 1.00 41.74 A ATOM 434 O PHE A 58 .610 15.528 4.141 1.00 40.63 AATOM 435 N LYS A 59 .034 16.823 2.389 1.00 42.14 A ATOM 436 CA LYS A 591.327 17.496 2.363 1.00 42.84 A ATOM 437 CB LYS A 59 1.445 18.441 1.1581.00 44.84 A ATOM 438 CG LYS A 59 1.444 17.756 −.206 1.00 47.75 A ATOM439 CD LYS A 59 1.788 18.739 −1.329 1.00 49.41 A ATOM 440 CE LYS A 591.789 18.050 −2.697 1.00 51.02 A ATOM 441 NZ LYS A 59 2.057 18.999−3.823 1.00 51.85 A ATOM 442 C LYS A 59 1.403 18.307 3.639 1.00 41.25 AATOM 443 O LYS A 59 2.446 18.388 4.278 1.00 40.75 A ATOM 444 N ARG A 60.274 18.898 4.005 1.00 40.74 A ATOM 445 CA ARG A 60 .198 19.713 5.2051.00 42.28 A ATOM 446 CB ARG A 60 −1.133 20.473 5.239 1.00 46.48 A ATOM447 CG ARG A 60 −1.243 21.564 4.174 1.00 51.56 A ATOM 448 CD ARG A 60−.227 22.673 4.426 1.00 56.26 A ATOM 449 NE ARG A 60 −.197 23.681 3.3641.00 60.76 A ATOM 450 CZ ARG A 60 .504 24.812 3.426 1.00 62.22 A ATOM451 NH1 ARG A 60 1.233 25.084 4.501 1.00 62.02 A ATOM 452 NH2 ARG A 60.486 25.670 2.412 1.00 62.68 A ATOM 453 C ARG A 60 .374 18.885 6.4751.00 40.66 A ATOM 454 O ARG A 60 .823 19.402 7.496 1.00 41.04 A ATOM 455N ILE A 61 .024 17.603 6.421 1.00 38.03 A ATOM 456 CA ILE A 61 .19216.746 7.590 1.00 34.21 A ATOM 457 CB ILE A 61 −.631 15.456 7.497 1.0032.45 A ATOM 458 CG2 ILE A 61 −.228 14.520 8.638 1.00 29.47 A ATOM 459CG1 ILE A 61 −2.127 15.776 7.548 1.00 31.31 A ATOM 460 CD1 ILE A 61−3.010 14.567 7.320 1.00 30.86 A ATOM 461 C ILE A 61 1.654 16.344 7.6891.00 33.40 A ATOM 462 O ILE A 61 2.230 16.326 8.773 1.00 30.59 A ATOM463 N CYS A 62 2.235 16.012 6.539 1.00 34.39 A ATOM 464 CA CYS A 623.630 15.605 6.469 1.00 36.39 A ATOM 465 CB CYS A 62 4.009 15.211 5.0351.00 35.67 A ATOM 466 SG CYS A 62 3.392 13.621 4.435 1.00 36.68 A ATOM467 C CYS A 62 4.543 16.736 6.937 1.00 37.23 A ATOM 468 O CYS A 62 5.53916.498 7.615 1.00 36.14 A ATOM 469 N GLU A 63 4.190 17.968 6.585 1.0038.33 A ATOM 470 CA GLU A 63 4.996 19.124 6.961 1.00 39.37 A ATOM 471 CBGLU A 63 4.608 20.325 6.097 1.00 41.87 A ATOM 472 CG GLU A 63 5.00820.131 4.637 1.00 44.04 A ATOM 473 CD GLU A 63 4.621 21.296 3.752 1.0045.93 A ATOM 474 OE1 GLU A 63 3.407 21.593 3.652 1.00 47.07 A ATOM 475OE2 GLU A 63 5.533 21.909 3.152 1.00 46.35 A ATOM 476 C GLU A 63 4.95719.483 8.442 1.00 37.95 A ATOM 477 O GLU A 63 5.798 20.250 8.915 1.0037.13 A ATOM 478 N ARG A 64 3.986 18.934 9.166 1.00 36.39 A ATOM 479 CAARG A 64 3.886 19.163 10.608 1.00 37.43 A ATOM 480 CB ARG A 64 2.42819.371 11.037 1.00 37.43 A ATOM 481 CG ARG A 64 1.829 20.731 10.710 1.0040.40 A ATOM 482 CD ARG A 64 .612 20.995 11.592 1.00 42.29 A ATOM 483 NEARG A 64 −.415 19.974 11.406 1.00 43.14 A ATOM 484 CZ ARG A 64 −1.19619.897 10.335 1.00 44.35 A ATOM 485 NH1 ARG A 64 −1.065 20.785 9.3601.00 44.07 A ATOM 486 NH2 ARG A 64 −2.103 18.933 10.234 1.00 44.06 AATOM 487 C ARG A 64 4.454 17.952 11.377 1.00 37.08 A ATOM 488 O ARG A 644.840 18.067 12.539 1.00 38.38 A ATOM 489 N SER A 65 4.506 16.801 10.7141.00 36.12 A ATOM 490 CA SER A 65 4.997 15.570 11.314 1.00 35.70 A ATOM491 CB SER A 65 5.048 14.464 10.265 1.00 35.60 A ATOM 492 OG SER A 656.067 14.711 9.310 1.00 34.83 A ATOM 493 C SER A 65 6.364 15.665 11.9821.00 36.13 A ATOM 494 O SER A 65 6.655 14.899 12.890 1.00 36.64 A ATOM495 N ALA A 66 7.207 16.593 11.540 1.00 36.59 A ATOM 496 CA ALA A 668.544 16.736 12.115 1.00 34.73 A ATOM 497 CB ALA A 66 8.451 16.91213.624 1.00 34.03 A ATOM 498 C ALA A 66 9.372 15.497 11.780 1.00 35.37 AATOM 499 O ALA A 66 10.364 15.199 12.444 1.00 37.03 A ATOM 500 N ILE A67 8.947 14.765 10.753 1.00 34.92 A ATOM 501 CA ILE A 67 9.651 13.56610.312 1.00 33.47 A ATOM 502 CB ILE A 67 8.673 12.386 10.079 1.00 30.76A ATOM 503 CG2 ILE A 67 9.438 11.146 9.666 1.00 29.23 A ATOM 504 CG1 ILEA 67 7.872 12.108 11.348 1.00 28.84 A ATOM 505 CD1 ILE A 67 6.788 11.06711.151 1.00 28.29 A ATOM 506 C ILE A 67 10.312 13.925 8.989 1.00 34.28 AATOM 507 O ILE A 67 9.624 14.239 8.017 1.00 36.16 A ATOM 508 N LYS A 6811.638 13.873 8.943 1.00 34.27 A ATOM 509 CA LYS A 68 12.352 14.2357.724 1.00 34.52 A ATOM 510 CB LYS A 68 13.688 14.891 8.090 1.00 35.42 AATOM 511 CG LYS A 68 13.505 16.015 9.091 1.00 41.45 A ATOM 512 CD LYS A68 14.753 16.865 9.328 1.00 44.25 A ATOM 513 CE LYS A 68 14.409 18.00610.300 1.00 45.99 A ATOM 514 NZ LYS A 68 15.554 18.899 10.677 1.00 46.24A ATOM 515 C LYS A 68 12.569 13.077 6.760 1.00 33.29 A ATOM 516 O LYS A68 12.737 13.287 5.555 1.00 33.72 A ATOM 517 N GLN A 69 12.560 11.8547.283 1.00 31.93 A ATOM 518 CA GLN A 69 12.756 10.679 6.441 1.00 30.12 AATOM 519 CB GLN A 69 14.211 10.591 5.963 1.00 32.01 A ATOM 520 CG GLN A69 15.208 10.263 7.060 1.00 34.66 A ATOM 521 CD GLN A 69 15.994 8.9896.779 1.00 37.65 A ATOM 522 OE1 GLN A 69 15.416 7.908 6.627 1.00 42.24 AATOM 523 NE2 GLN A 69 17.317 9.108 6.717 1.00 35.40 A ATOM 524 C GLN A69 12.410 9.400 7.174 1.00 27.55 A ATOM 525 O GLN A 69 12.518 9.3188.389 1.00 26.69 A ATOM 526 N ARG A 70 12.009 8.396 6.414 1.00 26.61 AATOM 527 CA ARG A 70 11.648 7.110 6.973 1.00 28.66 A ATOM 528 CB ARG A70 10.129 6.982 7.054 1.00 29.52 A ATOM 529 CG ARG A 70 9.441 7.9997.946 1.00 31.27 A ATOM 530 CD ARG A 70 7.912 7.856 7.848 1.00 32.64 AATOM 531 NE ARG A 70 7.373 8.476 6.636 1.00 31.85 A ATOM 532 CZ ARG A 706.126 8.330 6.190 1.00 33.49 A ATOM 533 NH1 ARG A 70 5.253 7.571 6.8441.00 33.87 A ATOM 534 NH2 ARG A 70 5.746 8.952 5.083 1.00 33.20 A ATOM535 C ARG A 70 12.202 6.021 6.065 1.00 28.42 A ATOM 536 O ARG A 7012.528 6.280 4.908 1.00 26.75 A ATOM 537 N TYR A 71 12.322 4.809 6.5961.00 28.10 A ATOM 538 CA TYR A 71 12.811 3.683 5.814 1.00 28.19 A ATOM539 CB TYR A 71 13.940 2.958 6.556 1.00 28.62 A ATOM 540 CG TYR A 7115.224 3.761 6.650 1.00 29.33 A ATOM 541 CD1 TYR A 71 15.475 4.597 7.7351.00 29.31 A ATOM 542 CE1 TYR A 71 16.651 5.341 7.812 1.00 31.09 A ATOM543 CD2 TYR A 71 16.180 3.690 5.643 1.00 28.03 A ATOM 544 CE2 TYR A 7117.350 4.426 5.710 1.00 30.76 A ATOM 545 CZ TYR A 71 17.581 5.248 6.7941.00 30.97 A ATOM 546 OH TYR A 71 18.748 5.974 6.847 1.00 34.98 A ATOM547 C TYR A 71 11.637 2.740 5.558 1.00 29.16 A ATOM 548 O TYR A 7111.068 2.161 6.486 1.00 26.84 A ATOM 549 N MET A 72 11.275 2.599 4.2881.00 28.94 A ATOM 550 CA MET A 72 10.147 1.773 3.907 1.00 27.84 A ATOM551 CB MET A 72 9.169 2.600 3.062 1.00 27.20 A ATOM 552 CG MET A 728.753 3.911 3.706 1.00 27.56 A ATOM 553 SD MET A 72 7.148 4.518 3.1441.00 22.93 A ATOM 554 CE MET A 72 6.139 3.616 4.227 1.00 26.94 A ATOM555 C MET A 72 10.528 .516 3.151 1.00 26.70 A ATOM 556 O MET A 72 11.360.551 2.241 1.00 25.56 A ATOM 557 N TYR A 73 9.918 −.597 3.549 1.00 24.06A ATOM 558 CA TYR A 73 10.147 −1.876 2.895 1.00 23.85 A ATOM 559 CB TYRA 73 9.463 −3.014 3.658 1.00 24.18 A ATOM 560 CG TYR A 73 9.171 −4.2172.779 1.00 24.55 A ATOM 561 CD1 TYR A 73 10.193 −5.055 2.348 1.00 21.59A ATOM 562 CE1 TYR A 73 9.928 −6.136 1.525 1.00 27.28 A ATOM 563 CD2 TYRA 73 7.869 −4.495 2.357 1.00 26.09 A ATOM 564 CE2 TYR A 73 7.594 −5.5811.531 1.00 26.05 A ATOM 565 CZ TYR A 73 8.630 −6.395 1.125 1.00 26.65 AATOM 566 OH TYR A 73 8.371 −7.483 .340 1.00 30.63 A ATOM 567 C TYR A 739.501 −1.756 1.531 1.00 24.72 A ATOM 568 O TYR A 73 10.066 −2.153 .5161.00 25.42 A ATOM 569 N LEU A 74 8.291 −1.220 1.529 1.00 24.58 A ATOM570 CA LEU A 74 7.547 −1.023 .297 1.00 27.00 A ATOM 571 CB LEU A 746.134 −.524 .597 1.00 26.63 A ATOM 572 CG LEU A 74 5.223 −1.486 1.3471.00 23.99 A ATOM 573 CD1 LEU A 74 4.071 −.711 1.932 1.00 24.50 A ATOM574 CD2 LEU A 74 4.749 −2.579 .420 1.00 23.90 A ATOM 575 C LEU A 748.242 .004 −.576 1.00 27.44 A ATOM 576 O LEU A 74 8.339 1.174 −.211 1.0026.38 A ATOM 577 N THR A 75 8.733 −.447 −1.724 1.00 29.33 A ATOM 578 CATHR A 75 9.385 .427 −2.685 1.00 28.26 A ATOM 579 CB THR A 75 10.624−.258 −3.316 1.00 27.99 A ATOM 580 OG1 THR A 75 10.243 −1.499 −3.9181.00 27.29 A ATOM 581 CG2 THR A 75 11.671 −.542 −2.260 1.00 30.37 A ATOM582 C THR A 75 8.331 .701 −3.764 1.00 29.52 A ATOM 583 O THR A 75 7.188.229 −3.664 1.00 25.85 A ATOM 584 N GLU A 76 8.699 1.464 −4.788 1.0030.38 A ATOM 585 CA GLU A 76 7.758 1.758 −5.853 1.00 31.86 A ATOM 586 CBGLU A 76 8.277 2.888 −6.730 1.00 34.29 A ATOM 587 CG GLU A 76 7.2273.361 −7.709 1.00 37.84 A ATOM 588 CD GLU A 76 7.774 4.305 −8.738 1.0040.62 A ATOM 589 OE1 GLU A 76 8.541 5.215 −8.359 1.00 41.20 A ATOM 590OE2 GLU A 76 7.422 4.144 −9.926 1.00 44.13 A ATOM 591 C GLU A 76 7.562.511 −6.707 1.00 32.06 A ATOM 592 O GLU A 76 6.453 .199 −7.154 1.0031.57 A ATOM 593 N GLU A 77 8.662 −.192 −6.936 1.00 30.45 A ATOM 594 CAGLU A 77 8.656 −1.412 −7.720 1.00 32.97 A ATOM 595 CB GLU A 77 10.080−1.949 −7.790 1.00 35.54 A ATOM 596 CG GLU A 77 10.284 −3.126 −8.7051.00 43.11 A ATOM 597 CD GLU A 77 11.767 −3.446 −8.885 1.00 46.08 A ATOM598 OE1 GLU A 77 12.485 −2.654 −9.543 1.00 47.40 A ATOM 599 OE2 GLU A 7712.218 −4.484 −8.358 1.00 47.34 A ATOM 600 C GLU A 77 7.727 −2.445−7.089 1.00 33.13 A ATOM 601 O GLU A 77 7.005 −3.150 −7.789 1.00 33.97 AATOM 602 N ILE A 78 7.737 −2.525 −5.761 1.00 32.98 A ATOM 603 CA ILE A78 6.890 −3.482 −5.045 1.00 33.29 A ATOM 604 CB ILE A 78 7.368 −3.668−3.584 1.00 32.97 A ATOM 605 CG2 ILE A 78 6.397 −4.556 −2.814 1.00 34.53A ATOM 606 CG1 ILE A 78 8.745 −4.330 −3.571 1.00 31.63 A ATOM 607 CD1ILE A 78 9.382 −4.396 −2.195 1.00 33.04 A ATOM 608 C ILE A 78 5.419−3.066 −5.051 1.00 34.05 A ATOM 609 O ILE A 78 4.544 −3.902 −5.262 1.0032.38 A ATOM 610 N LEU A 79 5.145 −1.782 −4.813 1.00 35.12 A ATOM 611 CALEU A 79 3.770 −1.297 −4.834 1.00 36.98 A ATOM 612 CB LEU A 79 3.698.167 −4.389 1.00 37.47 A ATOM 613 CG LEU A 79 3.811 .411 −2.887 1.0037.60 A ATOM 614 CD1 LEU A 79 3.898 1.899 −2.597 1.00 36.08 A ATOM 615CD2 LEU A 79 2.611 −.216 −2.202 1.00 35.79 A ATOM 616 C LEU A 79 3.191−1.433 −6.243 1.00 38.11 A ATOM 617 O LEU A 79 2.002 −1.705 −6.405 1.0039.23 A ATOM 618 N LYS A 80 4.038 −1.262 −7.257 1.00 39.10 A ATOM 619 CALYS A 80 3.600 −1.368 −8.649 1.00 40.27 A ATOM 620 CB LYS A 80 4.706−.885 −9.589 1.00 42.10 A ATOM 621 CG LYS A 80 4.913 .627 −9.598 1.0043.49 A ATOM 622 CD LYS A 80 4.325 1.294 −10.844 1.00 44.07 A ATOM 623CE LYS A 80 2.802 1.242 −10.867 1.00 46.55 A ATOM 624 NZ LYS A 80 2.2322.001 −12.020 1.00 47.24 A ATOM 625 C LYS A 80 3.171 −2.787 −9.043 1.0039.71 A ATOM 626 O LYS A 80 2.313 −2.958 −9.910 1.00 39.42 A ATOM 627 NLYS A 81 3.777 −3.799 −8.425 1.00 39.39 A ATOM 628 CA LYS A 81 3.420−5.188 −8.709 1.00 39.36 A ATOM 629 CB LYS A 81 4.599 −6.129 −8.454 1.0040.38 A ATOM 630 CG LYS A 81 5.848 −5.880 −9.269 1.00 42.46 A ATOM 631CD LYS A 81 6.940 −6.882 −8.883 1.00 44.35 A ATOM 632 CE LYS A 81 6.480−8.334 −9.111 1.00 45.75 A ATOM 633 NZ LYS A 81 7.512 −9.371 −8.780 1.0043.48 A ATOM 634 C LYS A 81 2.289 −5.598 −7.772 1.00 38.94 A ATOM 635 OLYS A 81 1.782 −6.711 −7.850 1.00 40.01 A ATOM 636 N ASN A 82 1.897−4.693 −6.884 1.00 39.20 A ATOM 637 CA ASN A 82 .849 −4.992 −5.918 1.0038.88 A ATOM 638 CB ASN A 82 1.475 −5.246 −4.543 1.00 38.01 A ATOM 639CG ASN A 82 2.231 −6.562 −4.482 1.00 36.74 A ATOM 640 OD1 ASN A 82 1.639−7.619 −4.291 1.00 35.51 A ATOM 641 ND2 ASN A 82 3.541 −6.500 −4.6631.00 34.42 A ATOM 642 C ASN A 82 −.193 −3.890 −5.807 1.00 38.13 A ATOM643 O ASN A 82 −.275 −3.195 −4.788 1.00 39.26 A ATOM 644 N PRO A 83−1.017 −3.724 −6.851 1.00 36.98 A ATOM 645 CD PRO A 83 −1.086 −4.574−8.051 1.00 34.43 A ATOM 646 CA PRO A 83 −2.069 −2.698 −6.867 1.00 37.02A ATOM 647 CB PRO A 83 −2.780 −2.957 −8.195 1.00 36.28 A ATOM 648 CG PROA 83 −2.530 −4.442 −8.435 1.00 34.63 A ATOM 649 C PRO A 83 −3.042 −2.735−5.673 1.00 37.05 A ATOM 650 O PRO A 83 −3.478 −1.686 −5.192 1.00 39.34A ATOM 651 N ASP A 84 −3.367 −3.930 −5.185 1.00 35.56 A ATOM 652 CA ASPA 84 −4.308 −4.062 −4.078 1.00 33.46 A ATOM 653 CB ASP A 84 −4.649−5.530 −3.853 1.00 34.51 A ATOM 654 CG ASP A 84 −5.314 −6.158 −5.0611.00 35.83 A ATOM 655 OD1 ASP A 84 −6.199 −5.499 −5.646 1.00 37.72 AATOM 656 OD2 ASP A 84 −4.961 −7.308 −5.420 1.00 37.56 A ATOM 657 C ASP A84 −3.845 −3.426 −2.774 1.00 33.39 A ATOM 658 O ASP A 84 −4.665 −2.968−1.982 1.00 31.87 A ATOM 659 N VAL A 85 −2.534 −3.411 −2.547 1.00 31.84A ATOM 660 CA VAL A 85 −1.970 −2.804 −1.349 1.00 29.40 A ATOM 661 CB VALA 85 −.464 −3.168 −1.201 1.00 31.38 A ATOM 662 CG1 VAL A 85 .244 −2.216−.222 1.00 32.10 A ATOM 663 CG2 VAL A 85. −.336 −4.600 −.718 1.00 29.20A ATOM 664 C VAL A 85 −2.134 −1.282 −1.449 1.00 29.43 A ATOM 665 O VAL A85 −2.082 −.574 −.445 1.00 26.13 A ATOM 666 N CYS A 86 −2.344 −.791−2.670 1.00 29.46 A ATOM 667 CA CYS A 86 −2.524 .638 −2.904 1.00 29.39 AATOM 668 CB CYS A 86 −2.097 1.001 −4.328 1.00 30.74 A ATOM 669 SG CYS A86 −.317 .843 −4.599 1.00 36.69 A ATOM 670 C CYS A 86 −3.953 1.107−2.664 1.00 29.64 A ATOM 671 O CYS A 86 −4.179 2.262 −2.306 1.00 30.15 AATOM 672 N ALA A 87 −4.925 .228 −2.864 1.00 26.40 A ATOM 673 CA ALA A 87−6.295 .642 −2.636 1.00 28.82 A ATOM 674 CB ALA A 87 −7.256 −.483 −2.9881.00 25.62 A ATOM 675 C ALA A 87 −6.429 1.031 −1.161 1.00 29.47 A ATOM676 O ALA A 87 −5.489 .881 −.385 1.00 29.21 A ATOM 677 N PHE A 88 −7.5911.548 −.779 1.00 30.50 A ATOM 678 CA PHE A 88 −7.817 1.946 .604 1.0031.87 A ATOM 679 CB PHE A 88 −8.753 3.157 .667 1.00 31.60 A ATOM 680 CGPHE A 88 −9.116 3.567 2.064 1.00 31.92 A ATOM 681 CD1 PHE A 88 −8.1273.926 2.979 1.00 32.89 A ATOM 682 CD2 PHE A 88 −10.443 3.592 2.471 1.0030.33 A ATOM 683 CE1 PHE A 88 −8.463 4.303 4.271 1.00 31.78 A ATOM 684CE2 PHE A 88 −10.786 3.967 3.761 1.00 30.31 A ATOM 685 CZ PHE A 88−9.798 4.323 4.663 1.00 30.55 A ATOM 686 C PHE A 88 −8.432 .775 1.3521.00 32.46 A ATOM 687 O PHE A 88 −7.846 .258 2.297 1.00 33.36 A ATOM 688N VAL A 89 −9.614 .358 .907 1.00 31.48 A ATOM 689 CA VAL A 89 −10.315−.759 1.518 1.00 31.02 A ATOM 690 CB VAL A 89 −11.000 −.330 2.835 1.0032.10 A ATOM 691 CG1 VAL A 89 −12.350 .336 2.543 1.00 30.78 A ATOM 692CG2 VAL A 89 −11.183 −1.527 3.737 1.00 33.25 A ATOM 693 C VAL A 89−11.377 −1.316 .563 1.00 30.23 A ATOM 694 O VAL A 89 −12.263 −2.036 .9971.00 26.54 A ATOM 695 N GLU A 90 −11.284 −.980 −.729 1.00 32.29 A ATOM696 CA GLU A 90 −12.246 −1.465 −1.729 1.00 32.87 A ATOM 697 CB GLU A 90−12.260 −.598 −2.989 1.00 35.11 A ATOM 698 CG GLU A 90 −12.132 .884−2.780 1.00 39.52 A ATOM 699 CD GLU A 90 −10.703 1.296 −2.502 1.00 40.81A ATOM 700 OE1 GLU A 90 −10.391 1.564 −1.326 1.00 44.46 A ATOM 701 OE2GLU A 90 −9.893 1.341 −3.457 1.00 42.34 A ATOM 702 C GLU A 90 −11.945−2.885 −2.166 1.00 32.49 A ATOM 703 O GLU A 90 −12.815 −3.577 −2.6631.00 32.58 A ATOM 704 N VAL A 91 −10.696 −3.311 −2.019 1.00 34.49 A ATOM705 CA VAL A 91 −10.318 −4.673 −2.384 1.00 34.27 A ATOM 706 CB VAL A 91−9.548 −4.719 −3.734 1.00 34.98 A ATOM 707 CG1 VAL A 91 −10.522 −4.597−4.887 1.00 36.02 A ATOM 708 CG2 VAL A 91 −8.528 −3.595 −3.805 1.0034.63 A ATOM 709 C VAL A 91 −9.450 −5.265 −1.282 1.00 34.25 A ATOM 710 OVAL A 91 −8.662 −4.553 −.650 1.00 36.76 A ATOM 711 N PRO A 92 −9.587−6.573 −1.022 1.00 32.30 A ATOM 712 CD PRO A 92 −10.508 −7.541 −1.6371.00 31.68 A ATOM 713 CA PRO A 92 −8.783 −7.210 .027 1.00 31.47 A ATOM714 CB PRO A 92 −9.387 −8.608 .120 1.00 28.44 A ATOM 715 CG PRO A 92−9.877 −8.851 −1.263 1.00 30.17 A ATOM 716 C PRO A 92 −7.282 −7.223−.286 1.00 30.77 A ATOM 717 O PRO A 92 −6.888 −7.231 −1.457 1.00 31.24 AATOM 718 N SER A 93 −6.450 −7.213 .756 1.00 29.04 A ATOM 719 CA SER A 93−5.000 −7.212 .560 1.00 28.86 A ATOM 720 CB SER A 93 −4.488 −5.774 .4061.00 27.99 A ATOM 721 OG SER A 93 −4.609 −5.050 1.615 1.00 24.98 A ATOM722 C SER A 93 −4.222 −7.900 1.679 1.00 28.57 A ATOM 723 O SER A 93−2.994 −7.841 1.710 1.00 30.63 A ATOM 724 N LEU A 94 −4.934 −8.567 2.5841.00 27.50 A ATOM 725 CA LEU A 94 −4.311 −9.263 3.712 1.00 24.56 A ATOM726 CB LEU A 94 −5.394 −9.949 4.558 1.00 22.81 A ATOM 727 CG LEU A 94−5.266 −10.012 6.088 1.00 24.83 A ATOM 728 CD1 LEU A 94 −5.765 −11.3756.568 1.00 20.33 A ATOM 729 CD2 LEU A 94 −3.824 −9.778 6.536 1.00 21.99A ATOM 730 C LEU A 94 −3.260 −10.310 3.295 1.00 23.22 A ATOM 731 O LEU A94 −2.144 −10.312 3.799 1.00 21.73 A ATOM 732 N ASP A 95 −3.631 −11.1982.381 1.00 22.41 A ATOM 733 CA ASP A 95 −2.733 −12.253 1.923 1.00 24.20A ATOM 734 CB ASP A 95 −3.446 −13.139 .896 1.00 25.44 A ATOM 735 CG ASPA 95 −4.614 −13.932 1.507 1.00 29.88 A ATOM 736 OD1 ASP A 95 −5.294−14.653 .749 1.00 34.47 A ATOM 737 OD2 ASP A 95 −4.851 −13.849 2.7371.00 29.62 A ATOM 738 C ASP A 95 −1.426 −11.727 1.356 1.00 24.33 A ATOM739 O ASP A 95 −.349 −12.190 1.731 1.00 24.02 A ATOM 740 N ALA A 96−1.515 −10.759 .451 1.00 24.12 A ATOM 741 CA ALA A 96 −.318 −10.173−.124 1.00 23.91 A ATOM 742 CB ALA A 96 −.685 −9.090 −1.113 1.00 24.59 AATOM 743 C ALA A 96 .550 −9.585 .975 1.00 25.17 A ATOM 744 O ALA A 961.776 −9.679 .906 1.00 28.05 A ATOM 745 N ARG A 97 −.076 −8.981 1.9871.00 22.01 A ATOM 746 CA ARG A 97 .679 −8.381 3.084 1.00 21.90 A ATOM747 CB ARG A 97 −.208 −7.447 3.911 1.00 20.08 A ATOM 748 CG ARG A 97−.695 −6.199 3.155 1.00 21.02 A ATOM 749 CD ARG A 97 −1.827 −5.559 3.9091.00 19.89 A ATOM 750 NE ARG A 97 −2.538 −4.543 3.141 1.00 24.71 A ATOM751 CZ ARG A 97 −2.095 −3.307 2.938 1.00 23.62 A ATOM 752 NH1 ARG A 97−.931 −2.931 3.443 1.00 23.02 A ATOM 753 NH2 ARG A 97 −2.832 −2.4402.254 1.00 25.63 A ATOM 754 C ARG A 97 1.315 −9.415 4.008 1.00 23.99 AATOM 755 O ARG A 97 2.438 −9.221 4.495 1.00 25.02 A ATOM 756 N GLN A 98.603 −10.510 4.255 1.00 22.43 A ATOM 757 CA GLN A 98 1.124 −11.538 5.1251.00 22.91 A ATOM 758 CB GLN A 98 .081 −12.645 5.340 1.00 21.13 A ATOM759 CG GLN A 98 −1.261 −12.154 5.938 1.00 20.57 A ATOM 760 CD GLN A 98−1.161 −11.687 7.391 1.00 19.43 A ATOM 761 OE1 GLN A 98 −1.797 −12.2548.283 1.00 19.15 A ATOM 762 NE2 GLN A 98 −.366 −10.654 7.630 1.00 15.68A ATOM 763 C GLN A 98 2.400 −12.097 4.504 1.00 24.91 A ATOM 764 O GLN A98 3.366 −12.364 5.218 1.00 24.11 A ATOM 765 N ALA A 99 2.410 −12.2383.174 1.00 26.86 A ATOM 766 CA ALA A 99 3.580 −12.766 2.455 1.00 28.83 AATOM 767 CB ALA A 99 3.268 −12.934 .961 1.00 28.35 A ATOM 768 C ALA A 994.764 −11.825 2.640 1.00 27.98 A ATOM 769 O ALA A 99 5.875 −12.258 2.9551.00 29.15 A ATOM 770 N MET A 100 4.515 −10.535 2.438 1.00 27.72 A ATOM771 CA MET A 100 5.537 −9.507 2.599 1.00 26.42 A ATOM 772 CB MET A 1004.941 −8.106 2.390 1.00 24.11 A ATOM 773 CG MET A 100 4.634 −7.739 .9401.00 24.57 A ATOM 774 SD MET A 100 3.735 −6.165 .749 1.00 18.38 A ATOM775 CE MET A 100 2.752 −6.545 −.586 1.00 21.64 A ATOM 776 C MET A 1006.096 −9.597 4.005 1.00 25.75 A ATOM 777 O MET A 100 7.305 −9.547 4.2031.00 24.42 A ATOM 778 N LEU A 101 5.194 −9.742 4.971 1.00 26.33 A ATOM779 CA LEU A 101 5.540 −9.819 6.388 1.00 27.46 A ATOM 780 CB LEU A 1014.262 −9.777 7.225 1.00 26.83 A ATOM 781 CG LEU A 101 4.012 −8.510 8.0291.00 29.59 A ATOM 782 CD1 LEU A 101 4.229 −7.300 7.144 1.00 30.34 A ATOM783 CD2 LEU A 101 2.600 −8.536 8.587 1.00 28.87 A ATOM 784 C LEU A 1016.349 −11.050 6.785 1.00 27.33 A ATOM 785 O LEU A 101 7.377 −10.9447.457 1.00 28.56 A ATOM 786 N ALA A 102 5.881 −12.218 6.371 1.00 25.00 AATOM 787 CA ALA A 102 6.560 −13.457 6.716 1.00 27.48 A ATOM 788 CB ALA A102 5.894 −14.627 5.994 1.00 23.71 A ATOM 789 C ALA A 102 8.056 −13.3956.381 1.00 28.69 A ATOM 790 O ALA A 102 8.870 −13.987 7.084 1.00 29.73 AATOM 791 N MET A 103 8.415 −12.661 5.329 1.00 29.35 A ATOM 792 CA MET A103 9.818 −12.560 4.924 1.00 32.04 A ATOM 793 CB MET A 103 9.941 −12.6623.401 1.00 34.43 A ATOM 794 CG MET A 103 9.850 −14.076 2.841 1.00 38.55A ATOM 795 SD MET A 103 11.158 −15.155 3.475 1.00 44.76 A ATOM 796 CEMET A 103 10.276 −16.041 4.747 1.00 39.47 A ATOM 797 C MET A 103 10.568−11.314 5.387 1.00 31.24 A ATOM 798 O MET A 103 11.695 −11.402 5.8641.00 31.61 A ATOM 799 N GLU A 104 9.951 −10.153 5.257 1.00 31.59 A ATOM800 CA GLU A 104 10.626 −8.915 5.630 1.00 31.31 A ATOM 801 CB GLU A 1049.865 −7.731 5.045 1.00 30.05 A ATOM 802 CG GLU A 104 10.553 −6.4065.240 1.00 32.44 A ATOM 803 CD GLU A 104 11.995 −6.407 4.762 1.00 33.01A ATOM 804 OE1 GLU A 104 12.390 −7.309 3.989 1.00 33.54 A ATOM 805 OE2GLU A 104 12.735 −5.485 5.158 1.00 33.64 A ATOM 806 C GLU A 104 10.900−8.671 7.118 1.00 30.88 A ATOM 807 O GLU A 104 11.992 −8.211 7.482 1.0029.95 A ATOM 808 N VAL A 105 9.926 −8.974 7.976 1.00 30.76 A ATOM 809 CAVAL A 105 10.085 −8.749 9.417 1.00 29.41 A ATOM 810 CB VAL A 105 8.766−8.996 10.161 1.00 28.39 A ATOM 811 CG1 VAL A 105 8.985 −8.867 11.6461.00 28.65 A ATOM 812 CG2 VAL A 105 7.715 −8.003 9.688 1.00 27.81 A ATOM813 C VAL A 105 11.199 −9.569 10.062 1.00 28.24 A ATOM 814 O VAL A 10511.977 −9.046 10.858 1.00 28.68 A ATOM 815 N PRO A 106 11.264 −10.8779.762 1.00 28.43 A ATOM 816 CD PRO A 106 10.166 −11.740 9.283 1.00 28.16A ATOM 817 CA PRO A 106 12.336 −11.688 10.357 1.00 25.95 A ATOM 818 CBPRO A 106 11.905 −13.120 10.035 1.00 25.33 A ATOM 819 CG PRO A 10610.418 −13.032 10.058 1.00 27.25 A ATOM 820 C PRO A 106 13.703 −11.3329.742 1.00 24.31 A ATOM 821 O PRO A 106 14.732 −11.423 10.400 1.00 20.89A ATOM 822 N ARG A 107 13.695 −10.934 8.473 1.00 24.37 A ATOM 823 CA ARGA 107 14.920 −10.556 7.785 1.00 29.22 A ATOM 824 CB ARG A 107 14.641−10.194 6.330 1.00 32.72 A ATOM 825 CG ARG A 107 15.902 −9.914 5.5101.00 36.87 A ATOM 826 CD ARG A 107 15.684 −8.778 4.525 1.00 40.02 A ATOM827 NE ARG A 107 15.873 −7.473 5.164 1.00 45.13 A ATOM 828 CZ ARG A 10715.466 −6.313 4.653 1.00 47.15 A ATOM 829 NH1 ARG A 107 14.832 −6.2823.488 1.00 50.56 A ATOM 830 NH2 ARG A 107 15.702 −5.181 5.304 1.00 47.09A ATOM 831 C ARG A 107 15.504 −9.341 8.485 1.00 28.90 A ATOM 832 O ARG A107 16.661 −9.357 8.908 1.00 29.13 A ATOM 833 N LEU A 108 14.695 −8.2898.616 1.00 28.98 A ATOM 834 CA LEU A 108 15.142 −7.067 9.280 1.00 28.70A ATOM 835 CB LEU A 108 14.043 −6.000 9.261 1.00 30.81 A ATOM 836 CG LEUA 108 14.376 −4.716 8.483 1.00 34.16 A ATOM 837 CD1 LEU A 108 13.264−3.690 8.653 1.00 33.94 A ATOM 838 CD2 LEU A 108 15.694 −4.138 8.9811.00 33.48 A ATOM 839 C LEU A 108 15.558 −7.350 10.716 1.00 26.96 A ATOM840 O LEU A 108 16.597 −6.879 11.170 1.00 27.32 A ATOM 841 N ALA A 10914.748 −8.124 11.429 1.00 25.77 A ATOM 842 CA ALA A 109 15.052 −8.47112.816 1.00 24.84 A ATOM 843 CB ALA A 109 13.973 −9.388 13.379 1.0026.69 A ATOM 844 C ALA A 109 16.409 −9.161 12.914 1.00 25.54 A ATOM 845O ALA A 109 17.164 −8.924 13.855 1.00 23.26 A ATOM 846 N LYS A 11016.710 −10.008 11.934 1.00 25.63 A ATOM 847 CA LYS A 110 17.966 −10.74511.917 1.00 27.86 A ATOM 848 CB LYS A 110 17.955 −11.805 10.811 1.0029.07 A ATOM 849 CG LYS A 110 19.306 −12.492 10.620 1.00 28.94 A ATOM850 CD LYS A 110 19.309 −13.385 9.389 1.00 30.99 A ATOM 851 CE LYS A 11020.569 −14.242 9.321 1.00 31.04 A ATOM 852 NZ LYS A 110 21.804 −13.4369.126 1.00 31.14 A ATOM 853 C LYS A 110 19.166 −9.831 11.716 1.00 28.05A ATOM 854 O LYS A 110 20.223 −10.049 12.296 1.00 28.69 A ATOM 855 N GLUA 111 19.011 −8.821 10.873 1.00 27.50 A ATOM 856 CA GLU A 111 20.100−7.897 10.622 1.00 28.58 A ATOM 857 CB GLU A 111 19.718 −6.956 9.4871.00 33.09 A ATOM 858 CG GLU A 111 20.666 −5.789 9.264 1.00 37.76 A ATOM859 CD GLU A 111 20.122 −4.809 8.231 1.00 41.62 A ATOM 860 OE1 GLU A 11119.723 −5.269 7.138 1.00 42.07 A ATOM 861 OE2 GLU A 111 20.094 −3.5868.512 1.00 45.45 A ATOM 862 C GLU A 111 20.407 −7.097 11.886 1.00 28.49A ATOM 863 O GLU A 111 21.571 −6.841 12.205 1.00 27.38 A ATOM 864 N ALAA 112 19.359 −6.720 12.612 1.00 26.03 A ATOM 865 CA ALA A 112 19.512−5.944 13.833 1.00 26.94 A ATOM 866 CB ALA A 112 18.143 −5.504 14.3541.00 28.28 A ATOM 867 C ALA A 112 20.241 −6.715 14.918 1.00 27.67 A ATOM868 O ALA A 112 21.086 −6.161 15.616 1.00 25.90 A ATOM 869 N ASP A 11319.918 −7.995 15.066 1.00 28.66 A ATOM 870 CA ASP A 113 20.551 −8.77516.109 1.00 29.69 A ATOM 871 CB ASP A 113 19.677 −9.961 16.490 1.0036.80 A ATOM 872 CG ASP A 113 18.955 −10.548 15.311 1.00 42.93 A ATOM873 OD1 ASP A 113 19.629 −10.976 14.352 1.00 47.19 A ATOM 874 OD2 ASP A113 17.707 −10.583 15.346 1.00 49.00 A ATOM 875 C ASP A 113 21.951−9.231 15.791 1.00 27.88 A ATOM 876 O ASP A 113 22.744 −9.424 16.6961.00 29.10 A ATOM 877 N GLU A 114 22.270 −9.411 14.520 1.00 27.42 A ATOM878 CA GLU A 114 23.629 −9.802 14.181 1.00 29.07 A ATOM 879 CB GLU A 11423.759 −10.072 12.679 1.00 32.21 A ATOM 880 CG GLU A 114 23.033 −11.34712.216 1.00 36.51 A ATOM 881 CD GLU A 114 23.752 −12.637 12.619 1.0037.69 A ATOM 882 OE1 GLU A 114 24.350 −12.673 13.715 1.00 38.62 A ATOM883 OE2 GLU A 114 23.710 −13.621 11.842 1.00 39.78 A ATOM 884 C GLU A114 24.514 −8.632 14.616 1.00 28.69 A ATOM 885 O GLU A 114 25.608 −8.83415.156 1.00 26.64 A ATOM 886 N LYS A 115 24.030 −7.409 14.394 1.00 28.82A ATOM 887 CA LYS A 115 24.757 −6.213 14.815 1.00 29.61 A ATOM 888 CBLYS A 115 24.007 −4.929 14.448 1.00 31.35 A ATOM 889 CG LYS A 115 24.182−4.438 13.028 1.00 33.87 A ATOM 890 CD LYS A 115 23.587 −3.040 12.8931.00 37.24 A ATOM 891 CE LYS A 115 23.869 −2.444 11.530 1.00 38.63 AATOM 892 NZ LYS A 115 23.370 −3.328 10.448 1.00 40.84 A ATOM 893 C LYS A115 24.863 −6.276 16.324 1.00 28.63 A ATOM 894 O LYS A 115 25.950 −6.21416.888 1.00 29.75 A ATOM 895 N ALA A 116 23.711 −6.412 16.971 1.00 28.40A ATOM 896 CA ALA A 116 23.637 −6.497 18.427 1.00 28.89 A ATOM 897 CBALA A 116 22.187 −6.743 18.864 1.00 29.26 A ATOM 898 C ALA A 116 24.538−7.605 18.976 1.00 28.49 A ATOM 899 O ALA A 116 25.285 −7.391 19.9311.00 29.43 A ATOM 900 N ILE A 117 24.462 −8.782 18.374 1.00 28.53 A ATOM901 CA ILE A 117 25.265 −9.910 18.829 1.00 31.21 A ATOM 902 CB ILE A 11725.027 −11.179 17.971 1.00 29.88 A ATOM 903 CG2 ILE A 117 25.823 −12.33918.538 1.00 28.55 A ATOM 904 CG1 ILE A 117 23.549 −11.577 17.997 1.0032.55 A ATOM 905 CD1 ILE A 117 23.062 −12.008 19.351 1.00 33.54 A ATOM906 C ILE A 117 26.738 −9.563 18.766 1.00 32.35 A ATOM 907 O ILE A 11727.474 −9.769 19.732 1.00 30.97 A ATOM 908 N GLN A 118 27.152 −9.02417.625 1.00 34.54 A ATOM 909 CA GLN A 118 28.544 −8.646 17.402 1.0037.18 A ATOM 910 CB GLN A 118 28.690 −7.981 16.039 1.00 40.03 A ATOM 911CG GLN A 118 30.113 −7.648 15.668 1.00 44.57 A ATOM 912 CD GLN A 11830.200 −7.018 14.300 1.00 47.69 A ATOM 913 OE1 GLN A 118 29.776 −7.61113.302 1.00 49.39 A ATOM 914 NE2 GLN A 118 30.748 −5.807 14.239 1.0049.45 A ATOM 915 C GLN A 118 29.112 −7.727 18.478 1.00 37.04 A ATOM 916O GLN A 118 30.203 −7.977 18.988 1.00 37.17 A ATOM 917 N GLU A 11928.380 −6.666 18.820 1.00 36.89 A ATOM 918 CA GLU A 119 28.828 −5.71519.846 1.00 36.40 A ATOM 919 CB GLU A 119 27.773 −4.638 20.082 1.0036.37 A ATOM 920 CG GLU A 119 28.216 −3.559 21.045 1.00 36.77 A ATOM 921CD GLU A 119 27.063 −2.710 21.534 1.00 38.45 A ATOM 922 OE1 GLU A 11926.097 −2.525 20.768 1.00 38.88 A ATOM 923 OE2 GLU A 119 27.132 −2.21322.677 1.00 38.52 A ATOM 924 C GLU A 119 29.071 −6.444 21.161 1.00 35.77A ATOM 925 O GLU A 119 30.134 −6.340 21.778 1.00 36.48 A ATOM 926 N TRPA 120 28.054 −7.177 21.580 1.00 35.05 A ATOM 927 CA TRP A 120 28.097−7.950 22.805 1.00 34.32 A ATOM 928 CB TRP A 120 26.802 −8.747 22.9031.00 31.27 A ATOM 929 CG TRP A 120 26.695 −9.670 24.050 1.00 29.64 AATOM 930 CD2 TRP A 120 26.228 −11.019 24.001 1.00 28.18 A ATOM 931 CE2TRP A 120 26.168 −11.486 25.328 1.00 28.95 A ATOM 932 CE3 TRP A 12025.849 −11.879 22.960 1.00 28.14 A ATOM 933 CD1 TRP A 120 26.903 −9.38025.365 1.00 27.98 A ATOM 934 NE1 TRP A 120 26.583 −10.464 26.141 1.0028.05 A ATOM 935 CZ2 TRP A 120 25.742 −12.788 25.647 1.00 30.03 A ATOM936 CZ3 TRP A 120 25.425 −13.172 23.278 1.00 30.61 A ATOM 937 CH2 TRP A120 25.378 −13.612 24.611 1.00 27.55 A ATOM 938 C TRP A 120 29.309−8.863 22.735 1.00 34.10 A ATOM 939 O TRP A 120 29.861 −9.269 23.7571.00 36.05 A ATOM 940 N GLY A 121 29.711 −9.178 21.510 1.00 34.61 A ATOM941 CA GLY A 121 30.864 −10.028 21.283 1.00 35.14 A ATOM 942 C GLY A 12130.900 −11.386 21.961 1.00 35.69 A ATOM 943 O GLY A 121 31.983 −11.91222.194 1.00 36.76 A ATOM 944 N GLN A 122 29.743 −11.960 22.273 1.0035.13 A ATOM 945 CA GLN A 122 29.683 −13.276 22.910 1.00 35.20 A ATOM946 CB GLN A 122 28.897 −13.209 24.224 1.00 35.80 A ATOM 947 CG GLN A122 29.639 −12.555 25.362 1.00 38.25 A ATOM 948 CD GLN A 122 30.903−13.313 25.745 1.00 40.71 A ATOM 949 OE1 GLN A 122 30.849 −14.458 26.2101.00 41.52 A ATOM 950 NE2 GLN A 122 32.050 −12.678 25.549 1.00 40.42 AATOM 951 C GLN A 122 29.022 −14.291 21.977 1.00 34.64 A ATOM 952 O GLN A122 28.359 −13.922 21.009 1.00 34.92 A ATOM 953 N SER A 123 29.205−15.571 22.268 1.00 33.07 A ATOM 954 CA SER A 123 28.622 −16.626 21.4491.00 33.33 A ATOM 955 CB SER A 123 28.974 −17.989 22.045 1.00 31.42 AATOM 956 OG SER A 123 28.341 −19.041 21.349 1.00 29.57 A ATOM 957 C SERA 123 27.103 −16.487 21.352 1.00 34.17 A ATOM 958 O SER A 123 26.471−15.885 22.220 1.00 35.47 A ATOM 959 N LYS A 124 26.529 −17.018 20.2761.00 35.18 A ATOM 960 CA LYS A 124 25.083 −16.992 20.093 1.00 33.65 AATOM 961 CB LYS A 124 24.689 −17.401 18.674 1.00 33.98 A ATOM 962 CG LYSA 124 24.815 −16.325 17.623 1.00 36.96 A ATOM 963 CD LYS A 124 24.322−16.850 16.280 1.00 37.21 A ATOM 964 CE LYS A 124 24.557 −15.840 15.1711.00 40.53 A ATOM 965 NZ LYS A 124 24.053 −14.487 15.527 1.00 40.81 AATOM 966 C LYS A 124 24.527 −18.021 21.060 1.00 32.99 A ATOM 967 O LYS A124 23.502 −17.791 21.707 1.00 31.91 A ATOM 968 N SER A 125 25.224−19.154 21.157 1.00 30.09 A ATOM 969 CA SER A 125 24.813 −20.243 22.0371.00 31.14 A ATOM 970 CB SER A 125 25.904 −21.328 22.104 1.00 30.57 AATOM 971 OG SER A 125 27.056 −20.885 22.806 1.00 29.74 A ATOM 972 C SERA 125 24.503 −19.733 23.438 1.00 29.64 A ATOM 973 O SER A 125 23.612−20.245 24.109 1.00 30.79 A ATOM 974 N GLY A 126 25.236 −18.712 23.8671.00 29.37 A ATOM 975 CA GLY A 126 25.018 −18.154 25.192 1.00 29.53 AATOM 976 C GLY A 126 23.653 −17.512 25.375 1.00 27.71 A ATOM 977 O GLY A126 23.261 −17.163 26.489 1.00 25.74 A ATOM 978 N ILE A 127 22.938−17.344 24.268 1.00 26.99 A ATOM 979 CA ILE A 127 21.605 −16.751 24.2871.00 25.17 A ATOM 980 CB ILE A 127 21.237 −16.221 22.886 1.00 22.05 AATOM 981 CG2 ILE A 127 19.752 −15.896 22.811 1.00 22.05 A ATOM 982 CG1ILE A 127 22.106 −15.001 22.577 1.00 18.84 A ATOM 983 CD1 ILE A 12721.862 −14.406 21.238 1.00 17.66 A ATOM 984 C ILE A 127 20.610 −17.81024.754 1.00 24.70 A ATOM 985 O ILE A 127 20.363 −18.790 24.060 1.0026.26 A ATOM 986 N THR A 128 20.047 −17.594 25.939 1.00 25.26 A ATOM 987CA THR A 128 19.101 −18.526 26.555 1.00 25.26 A ATOM 988 CB THR A 12819.418 −18.698 28.053 1.00 27.22 A ATOM 989 OG1 THR A 128 19.208 −17.44628.731 1.00 27.55 A ATOM 990 CG2 THR A 128 20.866 −19.134 28.245 1.0027.17 A ATOM 991 C THR A 128 17.646 −18.090 26.454 1.00 25.40 A ATOM 992O THR A 128 16.730 −18.854 26.798 1.00 24.68 A ATOM 993 N HIS A 12917.435 −16.857 26.007 1.00 22.77 A ATOM 994 CA HIS A 129 16.097 −16.30325.892 1.00 20.64 A ATOM 995 CB HIS A 129 15.762 −15.456 27.122 1.0018.09 A ATOM 996 CG HIS A 129 15.565 −16.245 28.378 1.00 21.09 A ATOM997 CD2 HIS A 129 14.433 −16.640 29.013 1.00 19.20 A ATOM 998 ND1 HIS A129 16.615 −16.724 29.130 1.00 18.25 A ATOM 999 CE1 HIS A 129 16.137−17.379 30.175 1.00 18.16 A ATOM 1000 NE2 HIS A 129 14.817 −17.34230.128 1.00 17.69 A ATOM 1001 C HIS A 129 15.975 −15.408 24.673 1.0022.13 A ATOM 1002 O HIS A 129 16.953 −14.800 24.243 1.00 21.06 A ATOM1003 N LEU A 130 14.762 −15.336 24.129 1.00 22.34 A ATOM 1004 CA LEU A130 14.463 −14.477 22.993 1.00 22.64 A ATOM 1005 CB LEU A 130 14.471−15.241 21.672 1.00 24.24 A ATOM 1006 CG LEU A 130 13.867 −14.417 20.5221.00 22.91 A ATOM 1007 CD1 LEU A 130 14.786 −13.246 20.200 1.00 24.49 AATOM 1008 CD2 LEU A 130 13.647 −15.289 19.303 1.00 21.22 A ATOM 1009 CLEU A 130 13.071 −13.894 23.199 1.00 24.28 A ATOM 1010 O LEU A 13012.117 −14.611 23.505 1.00 22.97 A ATOM 1011 N ILE A 131 12.978 −12.58023.051 1.00 23.85 A ATOM 1012 CA ILE A 131 11.718 −11.867 23.177 1.0022.17 A ATOM 1013 CB ILE A 131 11.752 −10.834 24.320 1.00 19.17 A ATOM1014 CG2 ILE A 131 10.523 −9.914 24.219 1.00 17.23 A ATOM 1015 CG1 ILE A131 11.822 −11.557 25.666 1.00 15.59 A ATOM 1016 CD1 ILE A 131 11.885−10.632 26.867 1.00 16.20 A ATOM 1017 C ILE A 131 11.572 −11.139 21.8561.00 22.74 A ATOM 1018 O ILE A 131 12.378 −10.260 21.537 1.00 24.68 AATOM 1019 N PHE A 132 10.571 −11.522 21.075 1.00 21.87 A ATOM 1020 CAPHE A 132 10.364 −10.896 19.788 1.00 22.84 A ATOM 1021 CB PHE A 13210.407 −11.935 18.658 1.00 25.22 A ATOM 1022 CG PHE A 132 10.347 −11.32717.282 1.00 26.03 A ATOM 1023 CD1 PHE A 132 9.126 −11.002 16.699 1.0027.91 A ATOM 1024 CD2 PHE A 132 11.516 −11.014 16.596 1.00 26.87 A ATOM1025 CE1 PHE A 132 9.074 −10.370 15.456 1.00 27.98 A ATOM 1026 CE2 PHE A132 11.469 −10.383 15.356 1.00 26.12 A ATOM 1027 CZ PHE A 132 10.249−10.061 14.787 1.00 27.33 A ATOM 1028 C PHE A 132 9.054 −10.142 19.7571.00 23.78 A ATOM 1029 O PHE A 132 8.020 −10.636 20.235 1.00 25.01 AATOM 1030 N CYS A 133 9.108 −8.948 19.176 1.00 21.79 A ATOM 1031 CA CYSA 133 7.951 −8.082 19.076 1.00 22.75 A ATOM 1032 CB CYS A 133 8.129−6.891 20.026 1.00 25.53 A ATOM 1033 SG CYS A 133 6.991 −5.537 19.7321.00 27.54 A ATOM 1034 C CYS A 133 7.676 −7.562 17.669 1.00 21.50 A ATOM1035 O CYS A 133 8.592 −7.180 16.940 1.00 22.97 A ATOM 1036 N SER A 1346.399 −7.533 17.309 1.00 21.18 A ATOM 1037 CA SER A 134 5.954 −7.03116.009 1.00 22.43 A ATOM 1038 CB SER A 134 6.173 −8.095 14.925 1.0022.07 A ATOM 1039 OG SER A 134 6.351 −7.508 13.641 1.00 21.45 A ATOM1040 C SER A 134 4.464 −6.733 16.168 1.00 24.43 A ATOM 1041 O SER A 1343.756 −7.503 16.838 1.00 24.55 A ATOM 1042 N THR A 135 3.977 −5.63715.580 1.00 24.20 A ATOM 1043 CA THR A 135 2.555 −5.313 15.716 1.0026.34 A ATOM 1044 CB THR A 135 2.107 −4.107 14.846 1.00 26.54 A ATOM1045 OG1 THR A 135 1.786 −4.562 13.530 1.00 28.93 A ATOM 1046 CG2 THR A135 3.199 −3.045 14.786 1.00 25.74 A ATOM 1047 C THR A 135 1.712 −6.53715.349 1.00 25.69 A ATOM 1048 O THR A 135 .660 −6.749 15.929 1.00 26.52A ATOM 1049 N THR A 136 2.168 −7.329 14.379 1.00 25.88 A ATOM 1050 CATHR A 136 1.479 −8.567 14.007 1.00 25.55 A ATOM 1051 CB THR A 136 .460−8.402 12.834 1.00 24.45 A ATOM 1052 OG1 THR A 136 1.149 −8.006 11.6481.00 22.72 A ATOM 1053 CG2 THR A 136 −.625 −7.396 13.173 1.00 25.44 AATOM 1054 C THR A 136 2.497 −9.623 13.558 1.00 25.00 A ATOM 1055 O THR A136 3.692 −9.343 13.416 1.00 23.29 A ATOM 1056 N THR A 137 2.004 −10.83913.360 1.00 24.15 A ATOM 1057 CA THR A 137 2.808 −11.957 12.875 1.0024.60 A ATOM 1058 CB THR A 137 3.378 −12.819 14.045 1.00 23.38 A ATOM1059 OG1 THR A 137 4.548 −13.503 13.580 1.00 25.80 A ATOM 1060 CG2 THR A137 2.370 −13.837 14.543 1.00 20.20 A ATOM 1061 C THR A 137 1.814−12.724 11.997 1.00 23.38 A ATOM 1062 O THR A 137 .676 −12.959 12.3931.00 21.68 A ATOM 1063 N PRO A 138 2.225 −13.099 10.781 1.00 24.14 AATOM 1064 CD PRO A 138 3.545 −12.846 10.175 1.00 23.44 A ATOM 1065 CAPRO A 138 1.347 −13.816 9.851 1.00 24.04 A ATOM 1066 CB PRO A 138 2.069−13.657 8.523 1.00 24.17 A ATOM 1067 CG PRO A 138 3.504 −13.700 8.9301.00 23.06 A ATOM 1068 C PRO A 138 .927 −15.259 10.100 1.00 24.49 A ATOM1069 O PRO A 138 −.168 −15.662 9.699 1.00 24.01 A ATOM 1070 N ASP A 1391.765 −16.043 10.757 1.00 24.32 A ATOM 1071 CA ASP A 139 1.427 −17.44310.959 1.00 26.63 A ATOM 1072 CB ASP A 139 2.227 −18.311 9.970 1.0030.30 A ATOM 1073 CG ASP A 139 2.354 −17.683 8.582 1.00 34.13 A ATOM1074 OD1 ASP A 139 3.341 −17.999 7.875 1.00 38.40 A ATOM 1075 OD2 ASP A139 1.474 −16.893 8.179 1.00 34.14 A ATOM 1076 C ASP A 139 1.741 −17.93812.358 1.00 26.12 A ATOM 1077 O ASP A 139 2.041 −17.175 13.270 1.0025.57 A ATOM 1078 N LEU A 140 1.654 −19.253 12.499 1.00 27.76 A ATOM1079 CA LEU A 140 2.002 −19.949 13.731 1.00 26.83 A ATOM 1080 CB LEU A140 .778 −20.555 14.399 1.00 28.40 A ATOM 1081 CG LEU A 140 −.177−19.538 15.008 1.00 30.52 A ATOM 1082 CD1 LEU A 140 −.928 −18.799 13.9041.00 32.48 A ATOM 1083 CD2 LEU A 140 −1.132 −20.254 15.923 1.00 30.95 AATOM 1084 C LEU A 140 2.929 −21.052 13.244 1.00 27.18 A ATOM 1085 O LEUA 140 2.548 −21.853 12.388 1.00 28.82 A ATOM 1086 N PRO A 141 4.160−21.104 13.766 1.00 25.78 A ATOM 1087 CD PRO A 141 5.159 −22.037 13.2161.00 25.32 A ATOM 1088 CA PRO A 141 4.766 −20.228 14.775 1.00 24.99 AATOM 1089 CB PRO A 141 6.107 −20.898 15.025 1.00 26.03 A ATOM 1090 CGPRO A 141 6.459 −21.422 13.661 1.00 26.03 A ATOM 1091 C PRO A 141 4.924−18.763 14.344 1.00 24.56 A ATOM 1092 O PRO A 141 4.825 −18.427 13.1621.00 23.75 A ATOM 1093 N GLY A 142 5.177 −17.894 15.313 1.00 24.62 AATOM 1094 CA GLY A 142 5.349 −16.490 15.009 1.00 23.80 A ATOM 1095 C GLYA 142 6.792 −16.180 14.679 1.00 26.14 A ATOM 1096 O GLY A 142 7.660−17.059 14.729 1.00 25.21 A ATOM 1097 N ALA A 143 7.041 −14.917 14.3521.00 25.92 A ATOM 1098 CA ALA A 143 8.363 −14.426 13.999 1.00 26.94 AATOM 1099 CB ALA A 143 8.299 −12.909 13.760 1.00 25.13 A ATOM 1100 C ALAA 143 9.471 −14.756 15.008 1.00 26.98 A ATOM 1101 O ALA A 143 10.650−14.690 14.665 1.00 29.10 A ATOM 1102 N ASP A 144 9.112 −15.085 16.2481.00 27.97 A ATOM 1103 CA ASP A 144 10.130 −15.435 17.241 1.00 28.11 AATOM 1104 CB ASP A 144 9.513 −15.650 18.643 1.00 28.84 A ATOM 1105 CGASP A 144 8.364 −16.668 18.662 1.00 29.51 A ATOM 1106 OD1 ASP A 1447.340 −16.426 17.994 1.00 27.31 A ATOM 1107 OD2 ASP A 144 8.480 −17.70319.364 1.00 30.81 A ATOM 1108 C ASP A 144 10.862 −16.697 16.784 1.0027.99 A ATOM 1109 O ASP A 144 12.100 −16.747 16.763 1.00 26.30 A ATOM1110 N PHE A 145 10.086 −17.711 16.406 1.00 26.99 A ATOM 1111 CA PHE A145 10.648 −18.968 15.930 1.00 27.15 A ATOM 1112 CB PHE A 145 9.536−19.933 15.544 1.00 27.87 A ATOM 1113 CG PHE A 145 10.027 −21.173 14.8581.00 28.08 A ATOM 1114 CD1 PHE A 145 10.427 −22.280 15.594 1.00 29.08 AATOM 1115 CD2 PHE A 145 10.108 −21.226 13.475 1.00 27.17 A ATOM 1116 CE1PHE A 145 10.902 −23.430 14.960 1.00 28.55 A ATOM 1117 CE2 PHE A 14510.580 −22.362 12.828 1.00 29.72 A ATOM 1118 CZ PHE A 145 10.979 −23.47213.575 1.00 27.75 A ATOM 1119 C PHE A 145 11.520 −18.711 14.710 1.0027.78 A ATOM 1120 O PHE A 145 12.690 −19.107 14.663 1.00 25.37 A ATOM1121 N GLU A 146 10.937 −18.041 13.723 1.00 28.13 A ATOM 1122 CA GLU A146 11.652 −17.746 12.504 1.00 28.43 A ATOM 1123 CB GLU A 146 10.763−16.982 11.538 1.00 32.67 A ATOM 1124 CG GLU A 146 10.552 −17.733 10.2371.00 39.15 A ATOM 1125 CD GLU A 146 10.033 −19.152 10.462 1.00 42.85 AATOM 1126 OE1 GLU A 146 8.847 −19.299 10.847 1.00 43.22 A ATOM 1127 OE2GLU A 146 10.816 −20.113 10.259 1.00 43.47 A ATOM 1128 C GLU A 14612.932 −16.983 12.730 1.00 27.87 A ATOM 1129 O GLU A 146 13.941 −17.28212.104 1.00 28.61 A ATOM 1130 N VAL A 147 12.900 −16.004 13.626 1.0026.97 A ATOM 1131 CA VAL A 147 14.087 −15.210 13.902 1.00 27.33 A ATOM1132 CB VAL A 147 13.757 −14.038 14.848 1.00 28.53 A ATOM 1133 CG1 VAL A147 15.024 −13.382 15.340 1.00 27.78 A ATOM 1134 CG2 VAL A 147 12.912−13.009 14.102 1.00 28.86 A ATOM 1135 C VAL A 147 15.154 −16.108 14.5091.00 27.76 A ATOM 1136 O VAL A 147 16.338 −15.976 14.199 1.00 26.81 AATOM 1137 N ALA A 148 14.721 −17.030 15.365 1.00 27.35 A ATOM 1138 CAALA A 148 15.630 −17.973 16.001 1.00 27.81 A ATOM 1139 CB ALA A 14814.878 −18.841 17.011 1.00 26.38 A ATOM 1140 C ALA A 148 16.252 −18.84914.923 1.00 28.55 A ATOM 1141 O ALA A 148 17.464 −19.061 14.895 1.0027.16 A ATOM 1142 N LYS A 149 15.409 −19.344 14.028 1.00 28.27 A ATOM1143 CA LYS A 149 15.865 −20.192 12.940 1.00 30.54 A ATOM 1144 CB LYS A149 14.655 −20.672 12.125 1.00 30.34 A ATOM 1145 CG LYS A 149 14.879−21.959 11.344 1.00 33.21 A ATOM 1146 CD LYS A 149 15.675 −21.726 10.0771.00 35.22 A ATOM 1147 CE LYS A 149 14.855 −20.955 9.054 1.00 36.29 AATOM 1148 NZ LYS A 149 15.631 −20.646 7.821 1.00 34.92 A ATOM 1149 C LYSA 149 16.885 −19.453 12.052 1.00 31.84 A ATOM 1150 O LYS A 149 17.946−20.000 11.752 1.00 33.57 A ATOM 1151 N LEU A 150 16.588 −18.223 11.6381.00 30.97 A ATOM 1152 CA LEU A 150 17.540 −17.480 10.804 1.00 31.42 AATOM 1153 CB LEU A 150 16.949 −16.151 10.311 1.00 33.16 A ATOM 1154 CGLEU A 150 16.023 −16.098 9.091 1.00 34.92 A ATOM 1155 CD1 LEU A 15014.652 −16.632 9.434 1.00 36.29 A ATOM 1156 CD2 LEU A 150 15.904 −14.6578.623 1.00 36.72 A ATOM 1157 C LEU A 150 18.811 −17.166 11.578 1.0030.60 A ATOM 1158 O LEU A 150 19.903 −17.155 11.020 1.00 31.87 A ATOM1159 N LEU A 151 18.665 −16.893 12.866 1.00 29.87 A ATOM 1160 CA LEU A151 19.809 −16.557 13.698 1.00 29.41 A ATOM 1161 CB LEU A 151 19.340−15.867 14.980 1.00 27.66 A ATOM 1162 CG LEU A 151 19.013 −14.378 14.8861.00 29.11 A ATOM 1163 CD1 LEU A 151 18.489 −13.880 16.225 1.00 26.30 AATOM 1164 CD2 LEU A 151 20.272 −13.620 14.468 1.00 28.44 A ATOM 1165 CLEU A 151 20.669 −17.763 14.061 1.00 29.68 A ATOM 1166 O LEU A 15121.799 −17.619 14.539 1.00 29.22 A ATOM 1167 N GLY A 152 20.140 −18.95513.826 1.00 29.85 A ATOM 1168 CA GLY A 152 20.886 −20.145 14.176 1.0029.71 A ATOM 1169 C GLY A 152 21.021 −20.159 15.687 1.00 29.47 A ATOM1170 O GLY A 152 22.076 −20.485 16.231 1.00 31.09 A ATOM 1171 N LEU A153 19.950 −19.766 16.367 1.00 26.59 A ATOM 1172 CA LEU A 153 19.947−19.743 17.814 1.00 24.43 A ATOM 1173 CB LEU A 153 18.747 −18.947 18.3261.00 25.57 A ATOM 1174 CG LEU A 153 19.004 −17.578 18.956 1.00 26.97 AATOM 1175 CD1 LEU A 153 19.894 −16.771 18.055 1.00 26.84 A ATOM 1176 CD2LEU A 153 17.682 −16.865 19.210 1.00 25.05 A ATOM 1177 C LEU A 15319.844 −21.190 18.241 1.00 23.58 A ATOM 1178 O LEU A 153 19.525 −22.05117.426 1.00 24.50 A ATOM 1179 N HIS A 154 20.124 −21.458 19.512 1.0025.47 A ATOM 1180 CA HIS A 154 20.063 −22.818 20.063 1.00 23.90 A ATOM1181 CB HIS A 154 20.640 −22.827 21.488 1.00 22.82 A ATOM 1182 CG HIS A154 20.888 −24.199 22.031 1.00 24.68 A ATOM 1183 CD2 HIS A 154 20.084−25.041 22.723 1.00 26.57 A ATOM 1184 ND1 HIS A 154 22.080 −24.86921.855 1.00 25.52 A ATOM 1185 CE1 HIS A 154 22.001 −26.064 22.414 1.0026.84 A ATOM 1186 NE2 HIS A 154 20.800 −26.194 22.949 1.00 28.28 A ATOM1187 C HIS A 154 18.612 −23.318 20.081 1.00 23.62 A ATOM 1188 O HIS A154 17.693 −22.576 20.407 1.00 21.68 A ATOM 1189 N PRO A 155 18.391−24.590 19.740 1.00 24.80 A ATOM 1190 CD PRO A 155 19.359 −25.673 19.5051.00 25.17 A ATOM 1191 CA PRO A 155 17.023 −25.109 19.739 1.00 25.08 AATOM 1192 CB PRO A 155 17.215 −26.578 19.371 1.00 25.18 A ATOM 1193 CGPRO A 155 18.576 −26.880 19.928 1.00 27.56 A ATOM 1194 C PRO A 15516.277 −24.932 21.058 1.00 26.29 A ATOM 1195 O PRO A 155 15.053 −24.97921.088 1.00 26.00 A ATOM 1196 N SER A 156 17.016 −24.729 22.143 1.0025.49 A ATOM 1197 CA SER A 156 16.392 −24.565 23.452 1.00 23.23 A ATOM1198 CB SER A 156 17.114 −25.424 24.500 1.00 24.30 A ATOM 1199 OG SER A156 16.916 −26.801 24.255 1.00 24.44 A ATOM 1200 C SER A 156 16.314−23.133 23.956 1.00 21.04 A ATOM 1201 O SER A 156 16.185 −22.911 25.1471.00 19.96 A ATOM 1202 N VAL A 157 16.429 −22.161 23.061 1.00 21.07 AATOM 1203 CA VAL A 157 16.314 −20.779 23.481 1.00 20.46 A ATOM 1204 CBVAL A 157 16.499 −19.753 22.308 1.00 18.81 A ATOM 1205 CG1 VAL A 15716.244 −18.331 22.828 1.00 19.92 A ATOM 1206 CG2 VAL A 157 17.899−19.826 21.737 1.00 22.14 A ATOM 1207 C VAL A 157 14.875 −20.662 23.9631.00 21.14 A ATOM 1208 O VAL A 157 13.962 −21.152 23.312 1.00 19.78 AATOM 1209 N LYS A 158 14.673 −20.035 25.110 1.00 20.85 A ATOM 1210 CALYS A 158 13.328 −19.855 25.622 1.00 22.35 A ATOM 1211 CB LYS A 15813.373 −19.711 27.141 1.00 23.13 A ATOM 1212 CG LYS A 158 13.667 −21.03027.858 1.00 25.41 A ATOM 1213 CD LYS A 158 13.697 −20.828 29.357 1.0024.19 A ATOM 1214 CE LYS A 158 15.117 −20.708 29.873 1.00 26.45 A ATOM1215 NZ LYS A 158 15.823 −22.024 29.939 1.00 25.92 A ATOM 1216 C LYS A158 12.798 −18.596 24.939 1.00 23.09 A ATOM 1217 O LYS A 158 13.164−17.480 25.291 1.00 21.21 A ATOM 1218 N ARG A 159 11.929 −18.799 23.9561.00 24.01 A ATOM 1219 CA ARG A 159 11.380 −17.710 23.155 1.00 24.63 AATOM 1220 CB ARG A 159 11.358 −18.128 21.676 1.00 25.38 A ATOM 1221 CGARG A 159 12.174 −19.388 21.376 1.00 27.28 A ATOM 1222 CD ARG A 15912.021 −19.830 19.935 1.00 29.70 A ATOM 1223 NE ARG A 159 10.669 −20.29319.622 1.00 29.95 A ATOM 1224 CZ ARG A 159 10.282 −21.565 19.619 1.0029.82 A ATOM 1225 NH1 ARG A 159 11.139 −22.533 19.916 1.00 30.94 A ATOM1226 NH2 ARG A 159 9.028 −21.868 19.313 1.00 33.57 A ATOM 1227 C ARG A159 9.982 −17.289 23.561 1.00 23.52 A ATOM 1228 O ARG A 159 9.217−18.080 24.097 1.00 25.02 A ATOM 1229 N VAL A 160 9.665 −16.024 23.3111.00 22.32 A ATOM 1230 CA VAL A 160 8.345 −15.474 23.595 1.00 21.08 AATOM 1231 CB VAL A 160 8.244 −14.796 24.984 1.00 22.06 A ATOM 1232 CG1VAL A 160 9.252 −13.676 25.105 1.00 21.67 A ATOM 1233 CG2 VAL A 1606.838 −14.249 25.175 1.00 19.10 A ATOM 1234 C VAL A 160 8.035 −14.43322.540 1.00 21.72 A ATOM 1235 O VAL A 160 8.852 −13.562 22.231 1.0020.95 A ATOM 1236 N GLY A 161 6.847 −14.528 21.976 1.00 21.41 A ATOM1237 CA GLY A 161 6.478 −13.560 20.967 1.00 22.25 A ATOM 1238 C GLY A161 5.433 −12.613 21.509 1.00 20.28 A ATOM 1239 O GLY A 161 4.449−13.044 22.117 1.00 20.06 A ATOM 1240 N VAL A 162 5.655 −11.322 21.3091.00 20.58 A ATOM 1241 CA VAL A 162 4.706 −10.314 21.769 1.00 22.29 AATOM 1242 CB VAL A 162 5.397 −9.253 22.691 1.00 21.30 A ATOM 1243 CG1VAL A 162 6.693 −8.821 22.104 1.00 24.10 A ATOM 1244 CG2 VAL A 162 4.501−8.056 22.885 1.00 21.27 A ATOM 1245 C VAL A 162 4.125 −9.656 20.5301.00 21.88 A ATOM 1246 O VAL A 162 4.769 −8.818 19.899 1.00 22.52 A ATOM1247 N PHE A 163 2.904 −10.050 20.179 1.00 21.80 A ATOM 1248 CA PHE A163 2.258 −9.516 18.989 1.00 20.47 A ATOM 1249 CB PHE A 163 2.004−10.663 18.012 1.00 21.66 A ATOM 1250 CG PHE A 163 3.212 −11.550 17.7921.00 22.63 A ATOM 1251 CD1 PHE A 163 4.364 −11.052 17.174 1.00 25.88 AATOM 1252 CD2 PHE A 163 3.206 −12.875 18.210 1.00 22.78 A ATOM 1253 CE1PHE A 163 5.495 −11.865 16.975 1.00 24.44 A ATOM 1254 CE2 PHE A 1634.329 −13.695 18.017 1.00 24.67 A ATOM 1255 CZ PHE A 163 5.472 −13.18717.398 1.00 21.69 A ATOM 1256 C PHE A 163 .960 −8.743 19.261 1.00 20.46A ATOM 1257 O PHE A 163 .251 −9.001 20.231 1.00 20.17 A ATOM 1258 N GLNA 164 .662 −7.787 18.390 1.00 19.59 A ATOM 1259 CA GLN A 164 −.538−6.954 18.500 1.00 21.23 A ATOM 1260 CB GLN A 164 −1.798 −7.767 18.1561.00 20.31 A ATOM 1261 CG GLN A 164 −1.650 −8.597 16.882 1.00 21.02 AATOM 1262 CD GLN A 164 −2.973 −8.990 16.228 1.00 23.06 A ATOM 1263 OE1GLN A 164 −2.985 −9.831 15.322 1.00 21.66 A ATOM 1264 NE2 GLN A 164−4.085 −8.380 16.666 1.00 19.73 A ATOM 1265 C GLN A 164 −.699 −6.25819.858 1.00 22.09 A ATOM 1266 O GLN A 164 −1.791 −6.189 20.425 1.0022.31 A ATOM 1267 N HIS A 165 .405 −5.748 20.382 1.00 22.18 A ATOM 1268CA HIS A 165 .354 −5.022 21.635 1.00 24.10 A ATOM 1269 CB HIS A 1651.592 −5.307 22.483 1.00 21.91 A ATOM 1270 CG HIS A 165 1.517 −6.59623.241 1.00 17.46 A ATOM 1271 CD2 HIS A 165 1.334 −6.842 24.559 1.0015.97 A ATOM 1272 ND1 HIS A 165 1.557 −7.827 22.623 1.00 16.67 A ATOM1273 CE1 HIS A 165 1.395 −8.776 23.527 1.00 17.09 A ATOM 1274 NE2 HIS A165 1.255 −8.206 24.710 1.00 15.95 A ATOM 1275 C HIS A 165 .292 −3.55621.215 1.00 27.28 A ATOM 1276 O HIS A 165 −.587 −2.812 21.642 1.00 26.92A ATOM 1277 N GLY A 166 1.211 −3.155 20.348 1.00 29.59 A ATOM 1278 CAGLY A 166 1.189 −1.787 19.877 1.00 33.81 A ATOM 1279 C GLY A 166 2.466−1.002 20.046 1.00 34.98 A ATOM 1280 O GLY A 166 3.506 −1.539 20.4361.00 36.81 A ATOM 1281 N CYS A 167 2.370 .287 19.748 1.00 35.13 A ATOM1282 CA CYS A 167 3.490 1.200 19.847 1.00 34.95 A ATOM 1283 CB CYS A 1673.049 2.604 19.435 1.00 36.37 A ATOM 1284 SG CYS A 167 2.675 2.79017.682 1.00 38.64 A ATOM 1285 C CYS A 167 4.102 1.257 21.238 1.00 34.59A ATOM 1286 O CYS A 167 5.198 1.782 21.402 1.00 36.85 A ATOM 1287 N PHEA 168 3.407 .729 22.240 1.00 32.51 A ATOM 1288 CA PHE A 168 3.936 .76123.603 1.00 31.87 A ATOM 1289 CB PHE A 168 2.781 .885 24.613 1.00 30.03A ATOM 1290 CG PHE A 168 1.954 −.362 24.758 1.00 30.47 A ATOM 1291 CD1PHE A 168 2.428 −1.451 25.477 1.00 29.65 A ATOM 1292 CD2 PHE A 168 .700−.454 24.165 1.00 30.86 A ATOM 1293 CE1 PHE A 168 1.662 −2.619 25.6041.00 28.73 A ATOM 1294 CE2 PHE A 168 −.073 −1.618 24.286 1.00 29.81 AATOM 1295 CZ PHE A 168 .413 −2.698 25.008 1.00 28.11 A ATOM 1296 C PHE A168 4.803 −.462 23.932 1.00 31.42 A ATOM 1297 O PHE A 168 5.464 −.50224.966 1.00 31.40 A ATOM 1298 N ALA A 169 4.797 −1.449 23.039 1.00 29.90A ATOM 1299 CA ALA A 169 5.554 −2.685 23.227 1.00 27.01 A ATOM 1300 CBALA A 169 5.299 −3.607 22.053 1.00 26.41 A ATOM 1301 C ALA A 169 7.067−2.512 23.444 1.00 26.73 A ATOM 1302 O ALA A 169 7.720 −3.369 24.0621.00 25.79 A ATOM 1303 N GLY A 170 7.623 −1.414 22.941 1.00 24.59 A ATOM1304 CA GLY A 170 9.047 −1.176 23.100 1.00 24.21 A ATOM 1305 C GLY A 1709.454 −1.313 24.551 1.00 25.87 A ATOM 1306 O GLY A 170 10.559 −1.77624.871 1.00 25.12 A ATOM 1307 N GLY A 171 8.540 −.918 25.433 1.00 25.08A ATOM 1308 CA GLY A 171 8.792 −1.002 26.852 1.00 25.49 A ATOM 1309 CGLY A 171 8.347 −2.307 27.489 1.00 25.76 A ATOM 1310 O GLY A 171 9.017−2.805 28.390 1.00 24.97 A ATOM 1311 N THR A 172 7.222 −2.869 27.0541.00 26.67 A ATOM 1312 CA THR A 172 6.768 −4.120 27.666 1.00 26.43 AATOM 1313 CB THR A 172 5.403 −4.619 27.094 1.00 25.00 A ATOM 1314 OG1THR A 172 5.588 −5.868 26.421 1.00 25.54 A ATOM 1315 CG2 THR A 172 4.819−3.626 26.142 1.00 22.87 A ATOM 1316 C THR A 172 7.841 −5.198 27.4591.00 27.23 A ATOM 1317 O THR A 172 8.014 −6.091 28.290 1.00 26.37 A ATOM1318 N VAL A 173 8.580 −5.106 26.360 1.00 27.56 A ATOM 1319 CA VAL A 1739.623 −6.088 26.122 1.00 29.17 A ATOM 1320 CB VAL A 173 10.179 −5.99624.693 1.00 29.87 A ATOM 1321 CG1 VAL A 173 11.413 −6.834 24.591 1.0033.23 A ATOM 1322 CG2 VAL A 173 9.142 −6.501 23.696 1.00 28.54 A ATOM1323 C VAL A 173 10.760 −5.914 27.136 1.00 29.10 A ATOM 1324 O VAL A 17311.349 −6.908 27.581 1.00 29.94 A ATOM 1325 N LEU A 174 11.062 −4.66827.508 1.00 26.46 A ATOM 1326 CA LEU A 174 12.107 −4.416 28.504 1.0025.15 A ATOM 1327 CB LEU A 174 12.472 −2.931 28.557 1.00 23.15 A ATOM1328 CG LEU A 174 13.226 −2.342 27.361 1.00 22.33 A ATOM 1329 CD1 LEU A174 13.316 −.839 27.523 1.00 22.43 A ATOM 1330 CD2 LEU A 174 14.612−2.955 27.254 1.00 23.94 A ATOM 1331 C LEU A 174 11.594 −4.874 29.8721.00 25.36 A ATOM 1332 O LEU A 174 12.360 −5.370 30.716 1.00 23.86 AATOM 1333 N ARG A 175 10.288 −4.713 30.071 1.00 23.61 A ATOM 1334 CA ARGA 175 9.635 −5.115 31.304 1.00 26.33 A ATOM 1335 CB ARG A 175 8.184−4.608 31.310 1.00 26.51 A ATOM 1336 CG ARG A 175 7.329 −5.182 32.4091.00 29.10 A ATOM 1337 CD ARG A 175 6.139 −4.287 32.726 1.00 31.57 AATOM 1338 NE ARG A 175 5.198 −4.159 31.620 1.00 34.18 A ATOM 1339 CZ ARGA 175 4.398 −5.132 31.196 1.00 35.28 A ATOM 1340 NH1 ARG A 175 4.422−6.323 31.783 1.00 37.05 A ATOM 1341 NH2 ARG A 175 3.554 −4.907 30.1981.00 35.45 A ATOM 1342 C ARG A 175 9.690 −6.646 31.394 1.00 26.56 A ATOM1343 O ARG A 175 9.846 −7.222 32.481 1.00 27.45 A ATOM 1344 N MET A 1769.584 −7.303 30.242 1.00 27.50 A ATOM 1345 CA MET A 176 9.644 −8.76430.193 1.00 27.64 A ATOM 1346 CB MET A 176 9.029 −9.278 28.879 1.0026.71 A ATOM 1347 CG MET A 176 7.521 −9.034 28.775 1.00 28.23 A ATOM1348 SD MET A 176 6.800 −9.487 27.195 1.00 23.55 A ATOM 1349 CE MET A176 7.101 −8.102 26.259 1.00 28.45 A ATOM 1350 C MET A 176 11.096 −9.22130.323 1.00 27.94 A ATOM 1351 O MET A 176 11.403 −10.166 31.052 1.0030.27 A ATOM 1352 N ALA A 177 11.987 −8.532 29.628 1.00 28.25 A ATOM1353 CA ALA A 177 13.403 −8.868 29.672 1.00 29.84 A ATOM 1354 CB ALA A177 14.200 −7.954 28.738 1.00 29.86 A ATOM 1355 C ALA A 177 13.961−8.767 31.075 1.00 30.68 A ATOM 1356 O ALA A 177 14.790 −9.592 31.4691.00 32.02 A ATOM 1357 N LYS A 178 13.528 −7.759 31.830 1.00 30.79 AATOM 1358 CA LYS A 178 14.038 −7.588 33.188 1.00 31.72 A ATOM 1359 CBLYS A 178 13.477 −6.310 33.830 1.00 31.12 A ATOM 1360 CG LYS A 17813.749 −6.197 35.345 1.00 29.02 A ATOM 1361 CD LYS A 178 13.189 −4.90335.918 1.00 29.04 A ATOM 1362 CE LYS A 178 13.136 −4.914 37.449 1.0027.26 A ATOM 1363 NZ LYS A 178 14.480 −4.807 38.065 1.00 28.61 A ATOM1364 C LYS A 178 13.706 −8.795 34.067 1.00 31.60 A ATOM 1365 O LYS A 17814.581 −9.355 34.733 1.00 31.68 A ATOM 1366 N ASP A 179 12.441 −9.20034.062 1.00 31.22 A ATOM 1367 CA ASP A 179 12.033 −10.329 34.880 1.0030.84 A ATOM 1368 CB ASP A 179 10.517 −10.497 34.829 1.00 31.04 A ATOM1369 CG ASP A 179 9.797 −9.640 35.859 1.00 35.44 A ATOM 1370 OD1 ASP A179 10.435 −8.734 36.452 1.00 30.14 A ATOM 1371 OD2 ASP A 179 8.581−9.875 36.070 1.00 37.43 A ATOM 1372 C ASP A 179 12.733 −11.607 34.4461.00 29.75 A ATOM 1373 O ASP A 179 13.051 −12.450 35.273 1.00 28.93 AATOM 1374 N LEU A 180 12.986 −11.744 33.151 1.00 28.74 A ATOM 1375 CALEU A 180 13.661 −12.936 32.651 1.00 28.44 A ATOM 1376 CB LEU A 18013.561 −13.009 31.132 1.00 25.80 A ATOM 1377 CG LEU A 180 12.197 −13.37930.563 1.00 25.86 A ATOM 1378 CD1 LEU A 180 12.387 −13.863 29.142 1.0026.09 A ATOM 1379 CD2 LEU A 180 11.575 −14.493 31.379 1.00 26.77 A ATOM1380 C LEU A 180 15.126 −12.981 33.060 1.00 29.17 A ATOM 1381 O LEU A180 15.590 −13.971 33.624 1.00 29.96 A ATOM 1382 N ALA A 181 15.852−11.901 32.787 1.00 29.52 A ATOM 1383 CA ALA A 181 17.273 −11.843 33.1161.00 28.81 A ATOM 1384 CB ALA A 181 17.909 −10.617 32.473 1.00 27.02 AATOM 1385 C ALA A 181 17.571 −11.850 34.614 1.00 29.43 A ATOM 1386 O ALAA 181 18.621 −12.323 35.037 1.00 29.28 A ATOM 1387 N GLU A 182 16.654−11.334 35.418 1.00 28.32 A ATOM 1388 CA GLU A 182 16.903 −11.283 36.8451.00 28.42 A ATOM 1389 CB GLU A 182 16.206 −10.057 37.446 1.00 28.31 AATOM 1390 CG GLU A 182 17.074 −8.799 37.425 1.00 28.39 A ATOM 1391 CDGLU A 182 16.286 −7.505 37.641 1.00 30.17 A ATOM 1392 OE1 GLU A 18215.276 −7.535 38.378 1.00 31.81 A ATOM 1393 OE2 GLU A 182 16.683 −6.45537.079 1.00 26.98 A ATOM 1394 C GLU A 182 16.533 −12.545 37.612 1.0029.49 A ATOM 1395 O GLU A 182 17.124 −12.827 38.657 1.00 29.42 A ATOM1396 N ASN A 183 15.587 −13.318 37.085 1.00 27.48 A ATOM 1397 CA ASN A183 15.139 −14.531 37.747 1.00 26.14 A ATOM 1398 CB ASN A 183 13.626−14.682 37.571 1.00 28.22 A ATOM 1399 CG ASN A 183 13.022 −15.678 38.5381.00 27.66 A ATOM 1400 OD1 ASN A 183 13.287 −15.633 39.740 1.00 26.28 AATOM 1401 ND2 ASN A 183 12.190 −16.571 38.023 1.00 29.55 A ATOM 1402 CASN A 183 15.844 −15.781 37.236 1.00 26.45 A ATOM 1403 O ASN A 18315.562 −16.896 37.690 1.00 25.91 A ATOM 1404 N ASN A 184 16.755 −15.59536.288 1.00 26.39 A ATOM 1405 CA ASN A 184 17.507 −16.710 35.715 1.0025.21 A ATOM 1406 CB ASN A 184 17.006 −17.015 34.305 1.00 23.95 A ATOM1407 CG ASN A 184 15.540 −17.407 34.285 1.00 26.13 A ATOM 1408 OD1 ASN A184 15.150 −18.407 34.888 1.00 27.10 A ATOM 1409 ND2 ASN A 184 14.719−16.618 33.595 1.00 24.91 A ATOM 1410 C ASN A 184 18.979 −16.346 35.6851.00 24.51 A ATOM 1411 O ASN A 184 19.439 −15.657 34.774 1.00 22.61 AATOM 1412 N ARG A 185 19.713 −16.793 36.701 1.00 25.18 A ATOM 1413 CAARG A 185 21.135 −16.489 36.792 1.00 26.91 A ATOM 1414 CB ARG A 18521.757 −17.152 38.027 1.00 27.36 A ATOM 1415 CG ARG A 185 23.194 −16.71238.326 1.00 27.62 A ATOM 1416 CD ARG A 185 23.915 −17.698 39.265 1.0029.15 A ATOM 1417 NE ARG A 185 23.236 −17.834 40.554 1.00 32.65 A ATOM1418 CZ ARG A 185 23.199 −16.886 41.491 1.00 32.73 A ATOM 1419 NH1 ARG A185 23.808 −15.718 41.298 1.00 34.52 A ATOM 1420 NH2 ARG A 185 22.543−17.102 42.623 1.00 32.17 A ATOM 1421 C ARG A 185 21.805 −17.000 35.5341.00 27.64 A ATOM 1422 O ARG A 185 21.583 −18.142 35.124 1.00 26.90 AATOM 1423 N GLY A 186 22.593 −16.131 34.907 1.00 29.73 A ATOM 1424 CAGLY A 186 23.301 −16.500 33.694 1.00 29.72 A ATOM 1425 C GLY A 18622.517 −16.302 32.408 1.00 28.96 A ATOM 1426 O GLY A 186 23.035 −16.51731.314 1.00 28.86 A ATOM 1427 N ALA A 187 21.267 −15.884 32.533 1.0027.00 A ATOM 1428 CA ALA A 187 20.423 −15.676 31.369 1.00 27.51 A ATOM1429 CB ALA A 187 18.968 −15.538 31.800 1.00 27.04 A ATOM 1430 C ALA A187 20.817 −14.463 30.547 1.00 28.01 A ATOM 1431 O ALA A 187 21.187−13.416 31.082 1.00 28.40 A ATOM 1432 N ARG A 188 20.724 −14.624 29.2361.00 27.77 A ATOM 1433 CA ARG A 188 21.006 −13.551 28.300 1.00 27.68 AATOM 1434 CB ARG A 188 22.331 −13.810 27.581 1.00 26.99 A ATOM 1435 CGARG A 188 23.572 −13.728 28.492 1.00 27.67 A ATOM 1436 CD ARG A 18823.868 −12.276 28.890 1.00 31.52 A ATOM 1437 NE ARG A 188 24.994 −12.15129.820 1.00 30.38 A ATOM 1438 CZ ARG A 188 24.909 −12.292 31.143 1.0031.58 A ATOM 1439 NH1 ARG A 188 23.741 −12.562 31.722 1.00 24.80 A ATOM1440 NH2 ARG A 188 26.002 −12.165 31.891 1.00 31.53 A ATOM 1441 C ARG A188 19.809 −13.538 27.321 1.00 28.85 A ATOM 1442 O ARG A 188 19.605−14.459 26.515 1.00 27.23 A ATOM 1443 N VAL A 189 18.993 −12.499 27.4361.00 27.60 A ATOM 1444 CA VAL A 189 17.819 −12.367 26.597 1.00 26.30 AATOM 1445 CB VAL A 189 16.676 −11.696 27.375 1.00 25.85 A ATOM 1446 CG1VAL A 189 15.384 −11.786 26.597 1.00 24.31 A ATOM 1447 CG2 VAL A 18916.519 −12.363 28.719 1.00 28.18 A ATOM 1448 C VAL A 189 18.122 −11.53925.360 1.00 25.71 A ATOM 1449 O VAL A 189 18.738 −10.485 25.438 1.0025.75 A ATOM 1450 N LEU A 190 17.723 −12.052 24.206 1.00 27.67 A ATOM1451 CA LEU A 190 17.889 −11.319 22.961 1.00 27.51 A ATOM 1452 CB LEU A190 18.196 −12.259 21.793 1.00 26.13 A ATOM 1453 CG LEU A 190 18.194−11.660 20.379 1.00 24.00 A ATOM 1454 CD1 LEU A 190 19.134 −10.44020.284 1.00 16.10 A ATOM 1455 CD2 LEU A 190 18.579 −12.758 19.394 1.0020.62 A ATOM 1456 C LEU A 190 16.519 −10.687 22.781 1.00 27.57 A ATOM1457 O LEU A 190 15.505 −11.383 22.709 1.00 29.76 A ATOM 1458 N VAL A191 16.491 −9.365 22.758 1.00 27.48 A ATOM 1459 CA VAL A 191 15.252−8.632 22.614 1.00 25.21 A ATOM 1460 CB VAL A 191 15.171 −7.544 23.6961.00 26.45 A ATOM 1461 CG1 VAL A 191 14.054 −6.574 23.376 1.00 26.55 AATOM 1462 CG2 VAL A 191 14.953 −8.198 25.072 1.00 23.22 A ATOM 1463 CVAL A 191 15.188 −8.022 21.218 1.00 25.89 A ATOM 1464 O VAL A 191 16.056−7.243 20.829 1.00 25.61 A ATOM 1465 N ILE A 192 14.162 −8.390 20.4601.00 25.32 A ATOM 1466 CA ILE A 192 14.026 −7.891 19.102 1.00 25.33 AATOM 1467 CB ILE A 192 14.340 −9.019 18.074 1.00 23.22 A ATOM 1468 CG2ILE A 192 14.375 −8.447 16.664 1.00 24.09 A ATOM 1469 CG1 ILE A 19215.700 −9.648 18.399 1.00 23.39 A ATOM 1470 CD1 ILE A 192 16.041 −10.88917.601 1.00 21.13 A ATOM 1471 C ILE A 192 12.654 −7.286 18.792 1.0027.03 A ATOM 1472 O ILE A 192 11.616 −7.857 19.117 1.00 28.27 A ATOM1473 N CYS A 193 12.676 −6.110 18.176 1.00 27.44 A ATOM 1474 CA CYS A193 11.459 −5.410 17.777 1.00 29.84 A ATOM 1475 CB CYS A 193 11.286−4.079 18.524 1.00 29.24 A ATOM 1476 SG CYS A 193 10.748 −4.211 20.2411.00 33.41 A ATOM 1477 C CYS A 193 11.616 −5.107 16.307 1.00 28.84 AATOM 1478 O CYS A 193 12.470 −4.301 15.939 1.00 27.97 A ATOM 1479 N SERA 194 10.803 −5.761 15.476 1.00 28.80 A ATOM 1480 CA SER A 194 10.844−5.541 14.036 1.00 28.93 A ATOM 1481 CB SER A 194 11.290 −6.816 13.3041.00 28.77 A ATOM 1482 OG SER A 194 11.556 −6.556 11.932 1.00 27.02 AATOM 1483 C SER A 194 9.462 −5.111 13.552 1.00 28.93 A ATOM 1484 O SER A194 8.457 −5.766 13.833 1.00 26.74 A ATOM 1485 N GLU A 195 9.425 −4.00512.816 1.00 29.64 A ATOM 1486 CA GLU A 195 8.172 −3.468 12.311 1.0030.24 A ATOM 1487 CB GLU A 195 7.737 −2.305 13.200 1.00 31.77 A ATOM1488 CG GLU A 195 7.727 −2.645 14.686 1.00 36.82 A ATOM 1489 CD GLU A195 6.410 −3.250 15.148 1.00 39.92 A ATOM 1490 OE1 GLU A 195 5.813−4.031 14.374 1.00 39.88 A ATOM 1491 OE2 GLU A 195 5.981 −2.948 16.2901.00 40.67 A ATOM 1492 C GLU A 195 8.278 −2.994 10.864 1.00 29.61 A ATOM1493 O GLU A 195 9.326 −2.519 10.426 1.00 28.59 A ATOM 1494 N THR A 1967.188 −3.141 10.118 1.00 28.84 A ATOM 1495 CA THR A 196 7.151 −2.6888.733 1.00 28.59 A ATOM 1496 CB THR A 196 7.561 −3.802 7.732 1.00 29.67A ATOM 1497 OG1 THR A 196 7.608 −3.250 6.412 1.00 27.60 A ATOM 1498 CG2THR A 196 6.558 −4.942 7.749 1.00 27.62 A ATOM 1499 C THR A 196 5.741−2.204 8.394 1.00 28.47 A ATOM 1500 O THR A 196 4.750 −2.732 8.902 1.0029.71 A ATOM 1501 N THR A 197 5.661 −1.194 7.536 1.00 26.20 A ATOM 1502CA THR A 197 4.390 −.632 7.139 1.00 23.42 A ATOM 1503 CB THR A 197 4.580.788 6.587 1.00 24.48 A ATOM 1504 OG1 THR A 197 5.705 .797 5.713 1.0024.80 A ATOM 1505 CG2 THR A 197 4.824 1.780 7.713 1.00 22.95 A ATOM 1506C THR A 197 3.666 −1.475 6.099 1.00 24.32 A ATOM 1507 O THR A 197 2.504−1.209 5.791 1.00 21.28 A ATOM 1508 N ALA A 198 4.341 −2.490 5.561 1.0023.32 A ATOM 1509 CA ALA A 198 3.731 −3.347 4.546 1.00 24.83 A ATOM 1510CB ALA A 198 4.631 −4.554 4.259 1.00 22.22 A ATOM 1511 C ALA A 198 2.327−3.827 4.944 1.00 27.02 A ATOM 1512 O ALA A 198 1.436 −3.939 4.099 1.0029.39 A ATOM 1513 N VAL A 199 2.129 −4.110 6.225 1.00 25.63 A ATOM 1514CA VAL A 199 .834 −4.581 6.697 1.00 25.98 A ATOM 1515 CB VAL A 199 1.001−5.406 7.999 1.00 27.15 A ATOM 1516 CG1 VAL A 199 1.506 −4.512 9.1241.00 26.01 A ATOM 1517 CG2 VAL A 199 −.319 −6.058 8.381 1.00 25.90 AATOM 1518 C VAL A 199 −.198 −3.459 6.943 1.00 27.11 A ATOM 1519 O VAL A199 −1.385 −3.736 7.171 1.00 24.23 A ATOM 1520 N THR A 200 .243 −2.2036.872 1.00 26.28 A ATOM 1521 CA THR A 200 −.649 −1.072 7.127 1.00 28.77A ATOM 1522 CB THR A 200 −.207 −.306 8.375 1.00 28.69 A ATOM 1523 OG1THR A 200 −1.236 .617 8.745 1.00 34.92 A ATOM 1524 CG2 THR A 200 1.082.468 8.100 1.00 29.34 A ATOM 1525 C THR A 200 −.812 −.046 6.003 1.0029.04 A ATOM 1526 O THR A 200 −1.803 .686 5.966 1.00 29.83 A ATOM 1527 NPHE A 201 .154 .013 5.093 1.00 29.37 A ATOM 1528 CA PHE A 201 .099 .9673.993 1.00 27.14 A ATOM 1529 CB PHE A 201 1.390 .900 3.164 1.00 26.36 AATOM 1530 CG PHE A 201 1.328 1.654 1.853 1.00 23.85 A ATOM 1531 CD1 PHEA 201 .634 1.131 .762 1.00 24.10 A ATOM 1532 CD2 PHE A 201 1.959 2.8891.713 1.00 24.80 A ATOM 1533 CE1 PHE A 201 .567 1.831 −.447 1.00 24.95 AATOM 1534 CE2 PHE A 201 1.901 3.597 .513 1.00 21.90 A ATOM 1535 CZ PHE A201 1.205 3.072 −.569 1.00 24.52 A ATOM 1536 C PHE A 201 −1.095 .7483.089 1.00 26.41 A ATOM 1537 O PHE A 201 −1.278 −.325 2.531 1.00 24.36 AATOM 1538 N ARG A 202 −1.900 1.789 2.941 1.00 24.97 A ATOM 1539 CA ARG A202 −3.063 1.730 2.075 1.00 24.55 A ATOM 1540 CB ARG A 202 −4.299 1.3272.883 1.00 20.28 A ATOM 1541 CG ARG A 202 −4.532 2.183 4.108 1.00 20.71A ATOM 1542 CD ARG A 202 −5.718 1.693 4.931 1.00 23.12 A ATOM 1543 NEARG A 202 −5.454 .417 5.588 1.00 24.02 A ATOM 1544 CZ ARG A 202 −5.566−.771 4.999 1.00 23.58 A ATOM 1545 NH1 ARG A 202 −5.942 −.855 3.736 1.0023.59 A ATOM 1546 NH2 ARG A 202 −5.305 −1.883 5.680 1.00 24.60 A ATOM1547 C ARG A 202 −3.251 3.116 1.448 1.00 24.73 A ATOM 1548 O ARG A 202−2.648 4.091 1.895 1.00 23.81 A ATOM 1549 N GLY A 203 −4.079 3.192 .4111.00 26.77 A ATOM 1550 CA GLY A 203 −4.339 4.458 −.251 1.00 27.86 A ATOM1551 C GLY A 203 −5.000 5.470 .666 1.00 29.95 A ATOM 1552 O GLY A 203−5.455 5.128 1.757 1.00 30.65 A ATOM 1553 N PRO A 204 −5.086 6.730 .2381.00 31.00 A ATOM 1554 CD PRO A 204 −4.681 7.238 −1.085 1.00 31.27 AATOM 1555 CA PRO A 204 −5.693 7.799 1.034 1.00 33.93 A ATOM 1556 CB PROA 204 −5.127 9.047 .388 1.00 33.92 A ATOM 1557 CG PRO A 204 −5.221 8.670−1.069 1.00 33.17 A ATOM 1558 C PRO A 204 −7.207 7.780 .961 1.00 35.37 AATOM 1559 O PRO A 204 −7.784 7.238 .028 1.00 38.01 A ATOM 1560 N SER A205 −7.846 8.387 1.945 1.00 37.66 A ATOM 1561 CA SER A 205 −9.295 8.4521.975 1.00 39.54 A ATOM 1562 CB SER A 205 −9.858 7.242 2.722 1.00 40.11A ATOM 1563 OG SER A 205 −11.271 7.211 2.638 1.00 45.37 A ATOM 1564 CSER A 205 −9.694 9.746 2.675 1.00 39.76 A ATOM 1565 O SER A 205 −9.10210.119 3.687 1.00 40.03 A ATOM 1566 N GLU A 206 −10.685 10.438 2.1291.00 41.11 A ATOM 1567 CA GLU A 206 −11.138 11.690 2.723 1.00 43.15 AATOM 1568 CB GLU A 206 −11.788 12.585 1.660 1.00 44.15 A ATOM 1569 CGGLU A 206 −12.678 11.861 .666 1.00 47.17 A ATOM 1570 CD GLU A 206−11.906 11.275 −.512 1.00 50.55 A ATOM 1571 OE1 GLU A 206 −11.174 10.273−.332 1.00 50.11 A ATOM 1572 OE2 GLU A 206 −12.031 11.830 −1.628 1.0051.91 A ATOM 1573 C GLU A 206 −12.100 11.481 3.895 1.00 43.15 A ATOM1574 O GLU A 206 −12.333 12.392 4.690 1.00 44.07 A ATOM 1575 N THR A 207−12.651 10.281 4.012 1.00 43.47 A ATOM 1576 CA THR A 207 −13.559 9.9985.109 1.00 43.94 A ATOM 1577 CB THR A 207 −14.742 9.123 4.639 1.00 46.32A ATOM 1578 OG1 THR A 207 −14.258 7.858 4.172 1.00 50.01 A ATOM 1579 CG2THR A 207 −15.494 9.814 3.511 1.00 47.66 A ATOM 1580 C THR A 207 −12.8319.297 6.260 1.00 42.70 A ATOM 1581 O THR A 207 −13.456 8.884 7.232 1.0042.48 A ATOM 1582 N HIS A 208 −11.509 9.183 6.155 1.00 41.66 A ATOM 1583CA HIS A 208 −10.709 8.520 7.185 1.00 40.56 A ATOM 1584 CB HIS A 208−10.471 7.071 6.761 1.00 40.63 A ATOM 1585 CG HIS A 208 −11.728 6.2726.641 1.00 41.45 A ATOM 1586 CD2 HIS A 208 −12.552 6.060 5.588 1.0041.71 A ATOM 1587 ND1 HIS A 208 −12.306 5.629 7.714 1.00 43.34 A ATOM1588 CE1 HIS A 208 −13.432 5.056 7.327 1.00 42.20 A ATOM 1589 NE2 HIS A208 −13.605 5.303 6.041 1.00 40.79 A ATOM 1590 C HIS A 208 −9.366 9.2167.468 1.00 40.72 A ATOM 1591 O HIS A 208 −8.305 8.578 7.455 1.00 36.97 AATOM 1592 N LEU A 209 −9.428 10.519 7.744 1.00 41.16 A ATOM 1593 CA LEUA 209 −8.240 11.328 8.013 1.00 42.25 A ATOM 1594 CB LEU A 209 −8.64812.766 8.322 1.00 44.19 A ATOM 1595 CG LEU A 209 −9.250 13.521 7.1301.00 45.60 A ATOM 1596 CD1 LEU A 209 −9.688 14.911 7.553 1.00 45.32 AATOM 1597 CD2 LEU A 209 −8.214 13.608 6.016 1.00 45.26 A ATOM 1598 C LEUA 209 −7.326 10.806 9.117 1.00 43.63 A ATOM 1599 O LEU A 209 −6.11711.059 9.100 1.00 43.18 A ATOM 1600 N ASP A 210 −7.885 10.077 10.0771.00 44.10 A ATOM 1601 CA ASP A 210 −7.054 9.538 11.144 1.00 43.86 AATOM 1602 CB ASP A 210 −7.921 8.879 12.224 1.00 44.72 A ATOM 1603 CG ASPA 210 −8.520 7.567 11.781 1.00 46.10 A ATOM 1604 OD1 ASP A 210 −8.9327.454 10.606 1.00 45.79 A ATOM 1605 OD2 ASP A 210 −8.595 6.649 12.6261.00 48.31 A ATOM 1606 C ASP A 210 −6.087 8.539 10.506 1.00 44.25 A ATOM1607 O ASP A 210 −4.962 8.352 10.985 1.00 44.96 A ATOM 1608 N SER A 211−6.521 7.928 9.402 1.00 42.15 A ATOM 1609 CA SER A 211 −5.700 6.9708.671 1.00 40.33 A ATOM 1610 CB SER A 211 −6.570 6.078 7.776 1.00 41.73A ATOM 1611 OG SER A 211 −5.763 5.245 6.948 1.00 40.95 A ATOM 1612 C SERA 211 −4.659 7.679 7.808 1.00 39.17 A ATOM 1613 O SER A 211 −3.592 7.1287.550 1.00 37.98 A ATOM 1614 N LEU A 212 −4.979 8.892 7.355 1.00 38.41 AATOM 1615 CA LEU A 212 −4.049 9.668 6.533 1.00 35.56 A ATOM 1616 CB LEUA 212 −4.622 11.048 6.201 1.00 34.77 A ATOM 1617 CG LEU A 212 −5.09111.392 4.787 1.00 33.15 A ATOM 1618 CD1 LEU A 212 −5.182 12.915 4.6681.00 32.90 A ATOM 1619 CD2 LEU A 212 −4.125 10.855 3.754 1.00 31.17 AATOM 1620 C LEU A 212 −2.792 9.857 7.358 1.00 35.22 A ATOM 1621 O LEU A212 −1.701 9.450 6.961 1.00 36.22 A ATOM 1622 N VAL A 213 −2.962 10.4998.510 1.00 33.04 A ATOM 1623 CA VAL A 213 −1.864 10.745 9.430 1.00 32.51A ATOM 1624 CB VAL A 213 −2.414 10.985 10.857 1.00 31.66 A ATOM 1625 CG1VAL A 213 −1.275 11.153 11.843 1.00 31.63 A ATOM 1626 CG2 VAL A 213−3.307 12.211 10.860 1.00 29.64 A ATOM 1627 C VAL A 213 −.911 9.5399.439 1.00 32.48 A ATOM 1628 O VAL A 213 .271 9.660 9.104 1.00 32.59 AATOM 1629 N GLY A 214 −1.449 8.378 9.809 1.00 31.64 A ATOM 1630 CA GLY A214 −.666 7.158 9.864 1.00 31.10 A ATOM 1631 C GLY A 214 .185 6.8858.638 1.00 31.81 A ATOM 1632 O GLY A 214 1.283 6.339 8.760 1.00 31.87 AATOM 1633 N GLN A 215 −.303 7.249 7.454 1.00 30.01 A ATOM 1634 CA GLN A215 .470 7.016 6.239 1.00 29.39 A ATOM 1635 CB GLN A 215 −.383 7.2494.990 1.00 29.12 A ATOM 1636 CG GLN A 215 −1.456 6.213 4.805 1.00 28.36A ATOM 1637 CD GLN A 215 −.938 4.825 5.120 1.00 29.65 A ATOM 1638 OE1GLN A 215 −1.545 4.095 5.899 1.00 27.40 A ATOM 1639 NE2 GLN A 215 .1954.458 4.523 1.00 29.22 A ATOM 1640 C GLN A 215 1.697 7.908 6.181 1.0029.72 A ATOM 1641 O GLN A 215 2.644 7.619 5.452 1.00 29.34 A ATOM 1642 NALA A 216 1.673 8.988 6.957 1.00 29.06 A ATOM 1643 CA ALA A 216 2.7819.928 6.977 1.00 29.34 A ATOM 1644 CB ALA A 216 2.250 11.358 6.959 1.0028.98 A ATOM 1645 C ALA A 216 3.711 9.744 8.167 1.00 28.44 A ATOM 1646 OALA A 216 4.859 10.171 8.119 1.00 28.77 A ATOM 1647 N LEU A 217 3.2269.105 9.225 1.00 26.41 A ATOM 1648 CA LEU A 217 4.037 8.934 10.417 1.0026.85 A ATOM 1649 CB LEU A 217 3.159 9.022 11.660 1.00 27.43 A ATOM 1650CG LEU A 217 2.419 10.340 11.889 1.00 27.77 A ATOM 1651 CD1 LEU A 2171.602 10.236 13.167 1.00 27.93 A ATOM 1652 CD2 LEU A 217 3.411 11.49511.970 1.00 28.42 A ATOM 1653 C LEU A 217 4.860 7.660 10.489 1.00 28.52A ATOM 1654 O LEU A 217 6.070 7.707 10.703 1.00 29.49 A ATOM 1655 N PHEA 218 4.196 6.524 10.324 1.00 28.61 A ATOM 1656 CA PHE A 218 4.853 5.22910.409 1.00 28.75 A ATOM 1657 CB PHE A 218 3.794 4.127 10.391 1.00 31.22A ATOM 1658 CG PHE A 218 2.703 4.324 11.403 1.00 34.00 A ATOM 1659 CD1PHE A 218 3.008 4.645 12.719 1.00 36.79 A ATOM 1660 CD2 PHE A 218 1.3704.170 11.046 1.00 36.49 A ATOM 1661 CE1 PHE A 218 2.002 4.811 13.6741.00 36.73 A ATOM 1662 CE2 PHE A 218 .347 4.333 11.993 1.00 38.04 A ATOM1663 CZ PHE A 218 .667 4.654 13.310 1.00 37.72 A ATOM 1664 C PHE A 2185.933 4.916 9.368 1.00 27.22 A ATOM 1665 O PHE A 218 5.798 5.219 8.1811.00 25.21 A ATOM 1666 N GLY A 219 7.011 4.300 9.851 1.00 28.13 A ATOM1667 CA GLY A 219 8.125 3.894 9.007 1.00 27.30 A ATOM 1668 C GLY A 2198.561 2.497 9.424 1.00 27.92 A ATOM 1669 O GLY A 219 7.950 1.909 10.3111.00 27.50 A ATOM 1670 N ASP A 220 9.615 1.968 8.805 1.00 28.69 A ATOM1671 CA ASP A 220 10.100 .626 9.123 1.00 27.97 A ATOM 1672 CB ASP A 22010.161 −.243 7.860 1.00 27.48 A ATOM 1673 CG ASP A 220 8.833 −.326 7.1381.00 28.81 A ATOM 1674 OD1 ASP A 220 7.811 .115 7.706 1.00 28.94 A ATOM1675 OD2 ASP A 220 8.810 −.848 6.003 1.00 30.23 A ATOM 1676 C ASP A 22011.470 .591 9.792 1.00 29.31 A ATOM 1677 O ASP A 220 12.346 1.412 9.5031.00 28.92 A ATOM 1678 N GLY A 221 11.648 −.388 10.678 1.00 29.62 A ATOM1679 CA GLY A 221 12.911 −.556 11.378 1.00 27.70 A ATOM 1680 C GLY A 22112.920 −1.746 12.328 1.00 26.08 A ATOM 1681 O GLY A 221 11.876 −2.27312.703 1.00 24.58 A ATOM 1682 N ALA A 222 14.114 −2.173 12.711 1.0026.01 A ATOM 1683 CA ALA A 222 14.270 −3.283 13.634 1.00 25.76 A ATOM1684 CB ALA A 222 14.657 −4.564 12.885 1.00 23.29 A ATOM 1685 C ALA A222 15.343 −2.915 14.644 1.00 27.10 A ATOM 1686 O ALA A 222 16.394−2.365 14.292 1.00 25.67 A ATOM 1687 N CYS A 223 15.071 −3.214 15.9061.00 27.08 A ATOM 1688 CA CYS A 223 16.016 −2.917 16.960 1.00 28.62 AATOM 1689 CB CYS A 223 15.413 −1.939 17.942 1.00 33.80 A ATOM 1690 SGCYS A 223 14.226 −2.768 18.964 1.00 42.48 A ATOM 1691 C CYS A 223 16.282−4.210 17.684 1.00 26.75 A ATOM 1692 O CYS A 223 15.392 −5.058 17.7831.00 25.04 A ATOM 1693 N ALA A 224 17.494 −4.347 18.212 1.00 24.80 AATOM 1694 CA ALA A 224 17.872 −5.560 18.923 1.00 26.10 A ATOM 1695 CBALA A 224 18.578 −6.529 17.975 1.00 21.48 A ATOM 1696 C ALA A 224 18.752−5.261 20.129 1.00 26.20 A ATOM 1697 O ALA A 224 19.707 −4.487 20.0571.00 23.62 A ATOM 1698 N LEU A 225 18.408 −5.901 21.240 1.00 28.73 AATOM 1699 CA LEU A 225 19.117 −5.738 22.499 1.00 29.59 A ATOM 1700 CBLEU A 225 18.213 −5.087 23.547 1.00 28.37 A ATOM 1701 CG LEU A 22517.447 −3.834 23.171 1.00 30.11 A ATOM 1702 CD1 LEU A 225 16.636 −3.37324.360 1.00 33.00 A ATOM 1703 CD2 LEU A 225 18.417 −2.757 22.733 1.0030.82 A ATOM 1704 C LEU A 225 19.541 −7.077 23.070 1.00 28.64 A ATOM1705 O LEU A 225 18.892 −8.099 22.837 1.00 26.77 A ATOM 1706 N ILE A 22620.629 −7.036 23.834 1.00 27.61 A ATOM 1707 CA ILE A 226 21.143 −8.18724.552 1.00 27.04 A ATOM 1708 CB ILE A 226 22.659 −8.443 24.267 1.0025.88 A ATOM 1709 CG2 ILE A 226 23.243 −9.389 25.305 1.00 27.04 A ATOM1710 CG1 ILE A 226 22.836 −9.095 22.899 1.00 25.32 A ATOM 1711 CD1 ILE A226 22.257 −10.490 22.817 1.00 24.29 A ATOM 1712 C ILE A 226 20.932−7.744 26.008 1.00 27.60 A ATOM 1713 O ILE A 226 21.506 −6.746 26.4631.00 26.23 A ATOM 1714 N VAL A 227 20.064 −8.455 26.718 1.00 27.92 AATOM 1715 CA VAL A 227 19.790 −8.127 28.109 1.00 29.45 A ATOM 1716 CBVAL A 227 18.280 −7.875 28.355 1.00 29.44 A ATOM 1717 CG1 VAL A 22717.995 −7.745 29.851 1.00 27.14 A ATOM 1718 CG2 VAL A 227 17.856 −6.60227.647 1.00 27.64 A ATOM 1719 C VAL A 227 20.274 −9.260 29.004 1.0030.44 A ATOM 1720 O VAL A 227 20.119 −10.441 28.677 1.00 30.38 A ATOM1721 N GLY A 228 20.878 −8.891 30.129 1.00 30.00 A ATOM 1722 CA GLY A228 21.381 −9.893 31.039 1.00 30.18 A ATOM 1723 C GLY A 228 21.795−9.294 32.354 1.00 31.31 A ATOM 1724 O GLY A 228 22.112 −8.109 32.4331.00 31.60 A ATOM 1725 N ALA A 229 21.774 −10.126 33.390 1.00 32.55 AATOM 1726 CA ALA A 229 22.160 −9.710 34.724 1.00 33.95 A ATOM 1727 CBALA A 229 21.252 −10.367 35.764 1.00 34.17 A ATOM 1728 C ALA A 22923.619 −10.111 34.961 1.00 35.33 A ATOM 1729 O ALA A 229 24.164 −10.97234.256 1.00 33.08 A ATOM 1730 N ASP A 230 24.248 −9.465 35.942 1.0036.86 A ATOM 1731 CA ASP A 230 25.640 −9.740 36.300 1.00 39.56 A ATOM1732 CB ASP A 230 25.757 −11.083 37.044 1.00 41.40 A ATOM 1733 CG ASP A230 24.520 −11.413 37.868 1.00 43.35 A ATOM 1734 OD1 ASP A 230 24.054−10.532 38.623 1.00 44.48 A ATOM 1735 OD2 ASP A 230 24.022 −12.56037.767 1.00 44.89 A ATOM 1736 C ASP A 230 26.532 −9.793 35.066 1.0039.71 A ATOM 1737 O ASP A 230 26.951 −10.873 34.651 1.00 39.33 A ATOM1738 N PRO A 231 26.831 −8.633 34.456 1.00 39.86 A ATOM 1739 CD PRO A231 26.381 −7.252 34.717 1.00 40.12 A ATOM 1740 CA PRO A 231 27.692−8.692 33.271 1.00 40.52 A ATOM 1741 CB PRO A 231 27.573 −7.280 32.6871.00 39.25 A ATOM 1742 CG PRO A 231 27.353 −6.433 33.884 1.00 38.53 AATOM 1743 C PRO A 231 29.136 −9.073 33.629 1.00 41.54 A ATOM 1744 O PROA 231 29.692 −8.570 34.605 1.00 43.36 A ATOM 1745 N ILE A 232 29.723−9.977 32.850 1.00 41.13 A ATOM 1746 CA ILE A 232 31.099 −10.420 33.0621.00 40.68 A ATOM 1747 CB ILE A 232 31.474 −11.530 32.070 1.00 40.34 AATOM 1748 CG2 ILE A 232 32.886 −11.998 32.333 1.00 38.27 A ATOM 1749 CG1ILE A 232 30.465 −12.675 32.178 1.00 39.77 A ATOM 1750 CD1 ILE A 23230.197 −13.355 30.861 1.00 41.07 A ATOM 1751 C ILE A 232 32.046 −9.23632.843 1.00 40.67 A ATOM 1752 O ILE A 232 32.089 −8.660 31.751 1.0039.36 A ATOM 1753 N PRO A 233 32.836 −8.882 33.872 1.00 41.83 A ATOM1754 CD PRO A 233 33.100 −9.709 35.064 1.00 41.56 A ATOM 1755 CA PRO A233 33.782 −7.762 33.803 1.00 42.38 A ATOM 1756 CB PRO A 233 34.560−7.888 35.108 1.00 42.80 A ATOM 1757 CG PRO A 233 34.539 −9.368 35.3651.00 42.88 A ATOM 1758 C PRO A 233 34.681 −7.788 32.589 1.00 42.20 AATOM 1759 O PRO A 233 35.137 −8.844 32.172 1.00 42.50 A ATOM 1760 N GLNA 234 34.914 −6.606 32.032 1.00 43.76 A ATOM 1761 CA GLN A 234 35.764−6.406 30.860 1.00 45.45 A ATOM 1762 CB GLN A 234 37.245 −6.416 31.2621.00 46.00 A ATOM 1763 CG GLN A 234 37.726 −7.729 31.838 1.00 48.56 AATOM 1764 CD GLN A 234 39.175 −7.678 32.263 1.00 49.12 A ATOM 1765 OE1GLN A 234 39.553 −6.892 33.128 1.00 50.98 A ATOM 1766 NE2 GLN A 23439.997 −8.520 31.656 1.00 49.92 A ATOM 1767 C GLN A 234 35.544 −7.39429.726 1.00 44.87 A ATOM 1768 O GLN A 234 36.397 −7.549 28.849 1.0045.60 A ATOM 1769 N VAL A 235 34.404 −8.071 29.756 1.00 44.58 A ATOM1770 CA VAL A 235 34.039 −9.028 28.720 1.00 43.67 A ATOM 1771 CB VAL A235 33.805 −10.440 29.299 1.00 44.91 A ATOM 1772 CG1 VAL A 235 33.227−11.353 28.218 1.00 45.45 A ATOM 1773 CG2 VAL A 235 35.115 −11.01029.822 1.00 45.12 A ATOM 1774 C VAL A 235 32.743 −8.524 28.108 1.0042.68 A ATOM 1775 O VAL A 235 32.571 −8.547 26.889 1.00 42.55 A ATOM1776 N GLU A 236 31.835 −8.076 28.975 1.00 40.47 A ATOM 1777 CA GLU A236 30.547 −7.527 28.551 1.00 39.21 A ATOM 1778 CB GLU A 236 29.380−8.321 29.133 1.00 35.88 A ATOM 1779 CG GLU A 236 29.437 −9.787 28.8441.00 34.44 A ATOM 1780 CD GLU A 236 28.341 −10.545 29.544 1.00 29.35 AATOM 1781 OE1 GLU A 236 28.117 −10.279 30.740 1.00 28.34 A ATOM 1782 OE2GLU A 236 27.718 −11.406 28.900 1.00 29.13 A ATOM 1783 C GLU A 23630.475 −6.112 29.082 1.00 39.21 A ATOM 1784 O GLU A 236 30.804 −5.86330.240 1.00 39.77 A ATOM 1785 N LYS A 237 30.041 −5.188 28.236 1.0040.00 A ATOM 1786 CA LYS A 237 29.946 −3.792 28.630 1.00 38.96 A ATOM1787 CB LYS A 237 30.721 −2.934 27.631 1.00 38.86 A ATOM 1788 CG LYS A237 30.876 −1.475 28.023 1.00 41.75 A ATOM 1789 CD LYS A 237 31.777−.743 27.024 1.00 44.57 A ATOM 1790 CE LYS A 237 31.936 .730 27.385 1.0045.75 A ATOM 1791 NZ LYS A 237 32.833 1.455 26.432 1.00 46.22 A ATOM1792 C LYS A 237 28.480 −3.377 28.676 1.00 38.35 A ATOM 1793 O LYS A 23727.786 −3.403 27.659 1.00 36.98 A ATOM 1794 N ALA A 238 28.006 −3.01929.865 1.00 37.12 A ATOM 1795 CA ALA A 238 26.625 −2.598 30.031 1.0035.90 A ATOM 1796 CB ALA A 238 26.131 −2.956 31.421 1.00 34.13 A ATOM1797 C ALA A 238 26.549 −1.094 29.811 1.00 36.34 A ATOM 1798 O ALA A 23827.546 −.386 29.977 1.00 37.36 A ATOM 1799 N CYS A 239 25.375 −.60829.415 1.00 35.65 A ATOM 1800 CA CYS A 239 25.179 .824 29.179 1.00 34.67A ATOM 1801 CB CYS A 239 25.042 1.096 27.682 1.00 34.03 A ATOM 1802 SGCYS A 239 23.884 .011 26.852 1.00 39.50 A ATOM 1803 C CYS A 239 23.9521.345 29.928 1.00 32.01 A ATOM 1804 O CYS A 239 23.922 2.488 30.384 1.0029.97 A ATOM 1805 N PHE A 240 22.952 .489 30.073 1.00 30.69 A ATOM 1806CA PHE A 240 21.731 .864 30.772 1.00 29.43 A ATOM 1807 CB PHE A 24020.651 1.222 29.753 1.00 27.09 A ATOM 1808 CG PHE A 240 21.002 2.39928.886 1.00 26.17 A ATOM 1809 CD1 PHE A 240 21.036 3.686 29.415 1.0025.93 A ATOM 1810 CD2 PHE A 240 21.323 2.223 27.544 1.00 28.55 A ATOM1811 CE1 PHE A 240 21.384 4.772 28.623 1.00 25.72 A ATOM 1812 CE2 PHE A240 21.673 3.314 26.743 1.00 23.97 A ATOM 1813 CZ PHE A 240 21.703 4.58327.285 1.00 23.90 A ATOM 1814 C PHE A 240 21.251 −.288 31.643 1.00 30.74A ATOM 1815 O PHE A 240 21.413 −1.447 31.277 1.00 32.77 A ATOM 1816 NGLU A 241 20.677 .021 32.802 1.00 31.99 A ATOM 1817 CA GLU A 241 20.147−1.025 33.678 1.00 34.57 A ATOM 1818 CB GLU A 241 20.852 −1.023 35.0461.00 35.81 A ATOM 1819 CG GLU A 241 22.360 −1.271 34.997 1.00 37.93 AATOM 1820 CD GLU A 241 23.006 −1.280 36.381 1.00 40.79 A ATOM 1821 OE1GLU A 241 22.690 −.392 37.211 1.00 42.12 A ATOM 1822 OE2 GLU A 24123.845 −2.170 36.638 1.00 42.83 A ATOM 1823 C GLU A 241 18.648 −.77133.867 1.00 34.22 A ATOM 1824 O GLU A 241 18.200 .382 33.877 1.00 34.52A ATOM 1825 N ILE A 242 17.877 −1.846 34.004 1.00 34.06 A ATOM 1826 CAILE A 242 16.434 −1.733 34.196 1.00 32.84 A ATOM 1827 CB ILE A 24215.670 −2.830 33.421 1.00 32.65 A ATOM 1828 CG2 ILE A 242 14.229 −2.38333.165 1.00 31.59 A ATOM 1829 CG1 ILE A 242 16.359 −3.113 32.089 1.0032.73 A ATOM 1830 CD1 ILE A 242 16.466 −1.903 31.191 1.00 33.02 A ATOM1831 C ILE A 242 16.124 −1.891 35.683 1.00 32.33 A ATOM 1832 O ILE A 24216.073 −3.009 36.199 1.00 34.81 A ATOM 1833 N VAL A 243 15.903 −.77036.362 1.00 30.43 A ATOM 1834 CA VAL A 243 15.624 −.761 37.795 1.0027.37 A ATOM 1835 CB VAL A 243 16.016 .621 38.394 1.00 28.23 A ATOM 1836CG1 VAL A 243 15.188 .923 39.626 1.00 22.92 A ATOM 1837 CG2 VAL A 24317.499 .632 38.740 1.00 29.02 A ATOM 1838 C VAL A 243 14.196 −1.09438.247 1.00 26.31 A ATOM 1839 O VAL A 243 14.000 −1.938 39.119 1.0025.11 A ATOM 1840 N TRP A 244 13.213 −.416 37.659 1.00 26.80 A ATOM 1841CA TRP A 244 11.806 −.578 38.033 1.00 25.99 A ATOM 1842 CB TRP A 24411.459 .445 39.123 1.00 24.69 A ATOM 1843 CG TRP A 244 10.085 .34439.686 1.00 26.65 A ATOM 1844 CD2 TRP A 244 8.923 1.064 39.252 1.0026.94 A ATOM 1845 CE2 TRP A 244 7.851 .655 40.071 1.00 28.19 A ATOM 1846CE3 TRP A 244 8.684 2.012 38.249 1.00 30.14 A ATOM 1847 CD1 TRP A 2449.681 −.448 40.715 1.00 27.61 A ATOM 1848 NE1 TRP A 244 8.342 −.26940.956 1.00 27.74 A ATOM 1849 CZ2 TRP A 244 6.554 1.163 39.923 1.0029.62 A ATOM 1850 CZ3 TRP A 244 7.387 2.517 38.100 1.00 31.77 A ATOM1851 CH2 TRP A 244 6.344 2.089 38.935 1.00 30.68 A ATOM 1852 C TRP A 24410.930 −.360 36.803 1.00 25.64 A ATOM 1853 O TRP A 244 11.230 .49935.968 1.00 24.94 A ATOM 1854 N THR A 245 9.837 −1.117 36.712 1.00 25.35A ATOM 1855 CA THR A 245 8.946 −1.064 35.554 1.00 25.32 A ATOM 1856 CBTHR A 245 9.110 −2.349 34.743 1.00 26.48 A ATOM 1857 OG1 THR A 245 8.406−2.238 33.509 1.00 28.56 A ATOM 1858 CG2 THR A 245 8.551 −3.538 35.5321.00 25.04 A ATOM 1859 C THR A 245 7.455 −.904 35.888 1.00 25.82 A ATOM1860 O THR A 245 7.029 −1.132 37.024 1.00 24.99 A ATOM 1861 N ALA A 2466.665 −.524 34.885 1.00 24.85 A ATOM 1862 CA ALA A 246 5.228 −.34635.067 1.00 23.46 A ATOM 1863 CB ALA A 246 4.957 .788 36.061 1.00 26.77A ATOM 1864 C ALA A 246 4.493 −.073 33.757 1.00 23.79 A ATOM 1865 O ALAA 246 5.073 .412 32.783 1.00 22.48 A ATOM 1866 N GLN A 247 3.205 −.39433.754 1.00 23.39 A ATOM 1867 CA GLN A 247 2.326 −.210 32.601 1.00 25.65A ATOM 1868 CB GLN A 247 2.155 −1.531 31.835 1.00 24.53 A ATOM 1869 CGGLN A 247 1.151 −1.473 30.682 1.00 24.31 A ATOM 1870 CD GLN A 247 .838−2.843 30.074 1.00 22.11 A ATOM 1871 OE1 GLN A 247 .257 −3.709 30.7261.00 23.16 A ATOM 1872 NE2 GLN A 247 1.224 −3.036 28.825 1.00 20.77 AATOM 1873 C GLN A 247 .984 .220 33.170 1.00 27.26 A ATOM 1874 O GLN A247 .569 −.263 34.222 1.00 28.63 A ATOM 1875 N THR A 248 .295 1.12532.494 1.00 28.56 A ATOM 1876 CA THR A 248 −.988 1.567 33.017 1.00 28.92A ATOM 1877 CB THR A 248 −.797 2.755 33.987 1.00 30.79 A ATOM 1878 OG1THR A 248 −1.944 2.862 34.842 1.00 35.24 A ATOM 1879 CG2 THR A 248 −.6154.060 33.211 1.00 31.01 A ATOM 1880 C THR A 248 −1.953 1.977 31.916 1.0027.53 A ATOM 1881 O THR A 248 −1.539 2.318 30.812 1.00 25.84 A ATOM 1882N VAL A 249 −3.241 1.925 32.226 1.00 25.93 A ATOM 1883 CA VAL A 249−4.272 2.318 31.279 1.00 27.96 A ATOM 1884 CB VAL A 249 −5.407 1.28831.251 1.00 28.05 A ATOM 1885 CG1 VAL A 249 −6.550 1.797 30.397 1.0027.80 A ATOM 1886 CG2 VAL A 249 −4.884 −.038 30.713 1.00 28.94 A ATOM1887 C VAL A 249 −4.825 3.679 31.713 1.00 27.45 A ATOM 1888 O VAL A 249−5.378 3.810 32.805 1.00 26.81 A ATOM 1889 N VAL A 250 −4.652 4.70030.880 1.00 27.86 A ATOM 1890 CA VAL A 250 −5.153 6.018 31.254 1.0028.83 A ATOM 1891 CB VAL A 250 −4.656 7.129 30.318 1.00 28.90 A ATOM1892 CG1 VAL A 250 −3.192 7.416 30.593 1.00 29.74 A ATOM 1893 CG2 VAL A250 −4.834 6.717 28.889 1.00 30.61 A ATOM 1894 C VAL A 250 −6.670 5.96831.235 1.00 28.87 A ATOM 1895 O VAL A 250 −7.274 5.444 30.301 1.00 27.18A ATOM 1896 N PRO A 251 −7.302 6.513 32.283 1.00 28.95 A ATOM 1897 CDPRO A 251 −6.680 7.371 33.302 1.00 27.77 A ATOM 1898 CA PRO A 251 −8.7606.530 32.405 1.00 30.93 A ATOM 1899 CB PRO A 251 −8.991 7.390 33.6431.00 28.74 A ATOM 1900 CG PRO A 251 −7.799 8.286 33.662 1.00 30.42 AATOM 1901 C PRO A 251 −9.479 7.053 31.168 1.00 33.62 A ATOM 1902 O PRO A251 −8.942 7.863 30.409 1.00 34.58 A ATOM 1903 N ASN A 252 −10.692 6.55030.970 1.00 36.56 A ATOM 1904 CA ASN A 252 −11.546 6.917 29.851 1.0038.78 A ATOM 1905 CB ASN A 252 −12.471 8.052 30.291 1.00 40.73 A ATOM1906 CG ASN A 252 −13.412 8.486 29.198 1.00 44.33 A ATOM 1907 OD1 ASN A252 −13.037 9.262 28.321 1.00 46.53 A ATOM 1908 ND2 ASN A 252 −14.6427.978 29.232 1.00 45.05 A ATOM 1909 C ASN A 252 −10.776 7.295 28.5791.00 38.09 A ATOM 1910 O ASN A 252 −10.867 8.427 28.106 1.00 38.27 AATOM 1911 N SER A 253 −10.044 6.331 28.016 1.00 36.57 A ATOM 1912 CA SERA 253 −9.236 6.568 26.816 1.00 36.26 A ATOM 1913 CB SER A 253 −7.7756.719 27.216 1.00 34.68 A ATOM 1914 OG SER A 253 −7.312 5.503 27.7781.00 32.19 A ATOM 1915 C SER A 253 −9.329 5.455 25.761 1.00 36.96 A ATOM1916 O SER A 253 −8.391 5.232 24.998 1.00 36.84 A ATOM 1917 N GLU A 254−10.455 4.762 25.719 1.00 37.92 A ATOM 1918 CA GLU A 254 −10.658 3.67824.766 1.00 38.18 A ATOM 1919 CB GLU A 254 −11.874 2.865 25.196 1.0040.81 A ATOM 1920 CG GLU A 254 −11.709 1.362 25.110 1.00 44.37 A ATOM1921 CD GLU A 254 −12.993 .637 25.461 1.00 44.94 A ATOM 1922 OE1 GLU A254 −13.494 .833 26.591 1.00 46.54 A ATOM 1923 OE2 GLU A 254 −13.507−.118 24.607 1.00 45.46 A ATOM 1924 C GLU A 254 −10.872 4.196 23.3421.00 37.96 A ATOM 1925 O GLU A 254 −11.532 5.217 23.127 1.00 34.76 AATOM 1926 N GLY A 255 −10.319 3.479 22.368 1.00 35.90 A ATOM 1927 CA GLYA 255 −10.487 3.881 20.985 1.00 34.05 A ATOM 1928 C GLY A 255 −9.5324.966 20.536 1.00 33.62 A ATOM 1929 O GLY A 255 −9.456 5.283 19.348 1.0034.14 A ATOM 1930 N ALA A 256 −8.806 5.549 21.482 1.00 32.67 A ATOM 1931CA ALA A 256 −7.844 6.588 21.145 1.00 31.58 A ATOM 1932 CB ALA A 256−7.138 7.081 22.399 1.00 30.56 A ATOM 1933 C ALA A 256 −6.840 6.00120.169 1.00 30.51 A ATOM 1934 O ALA A 256 −6.523 6.610 19.155 1.00 32.75A ATOM 1935 N ILE A 257 −6.348 4.808 20.482 1.00 29.54 A ATOM 1936 CAILE A 257 −5.383 4.115 19.635 1.00 28.79 A ATOM 1937 CB ILE A 257 −3.9714.131 20.255 1.00 28.12 A ATOM 1938 CG2 ILE A 257 −2.973 3.501 19.3001.00 28.32 A ATOM 1939 CG1 ILE A 257 −3.553 5.567 20.566 1.00 26.99 AATOM 1940 CD1 ILE A 257 −2.172 5.686 21.172 1.00 22.94 A ATOM 1941 C ILEA 257 −5.829 2.662 19.477 1.00 29.98 A ATOM 1942 O ILE A 257 −6.1281.976 20.457 1.00 31.42 A ATOM 1943 N GLY A 258 −5.882 2.193 18.239 1.0031.11 A ATOM 1944 CA GLY A 258 −6.300 .826 18.003 1.00 27.25 A ATOM 1945C GLY A 258 −6.105 .422 16.561 1.00 27.85 A ATOM 1946 O GLY A 258 −5.8511.259 15.682 1.00 24.88 A ATOM 1947 N GLY A 259 −6.223 −.879 16.324 1.0026.06 A ATOM 1948 CA GLY A 259 −6.054 −1.401 14.987 1.00 24.94 A ATOM1949 C GLY A 259 −6.788 −2.709 14.848 1.00 25.74 A ATOM 1950 O GLY A 259−6.904 −3.474 15.804 1.00 27.81 A ATOM 1951 N LYS A 260 −7.280 −2.97213.648 1.00 24.91 A ATOM 1952 CA LYS A 260 −8.022 −4.191 13.392 1.0024.18 A ATOM 1953 CB LYS A 260 −9.468 −3.834 13.058 1.00 23.37 A ATOM1954 CG LYS A 260 −10.120 −2.976 14.105 1.00 21.02 A ATOM 1955 CD LYS A260 −11.477 −2.506 13.624 1.00 27.51 A ATOM 1956 CE LYS A 260 −12.267−1.873 14.757 1.00 27.39 A ATOM 1957 NZ LYS A 260 −12.506 −2.874 15.8351.00 30.72 A ATOM 1958 C LYS A 260 −7.402 −4.988 12.256 1.00 23.16 AATOM 1959 O LYS A 260 −7.139 −4.452 11.185 1.00 26.09 A ATOM 1960 N VALA 261 −7.152 −6.265 12.496 1.00 22.53 A ATOM 1961 CA VAL A 261 −6.581−7.112 11.458 1.00 22.47 A ATOM 1962 CB VAL A 261 −5.764 −8.275 12.0561.00 22.44 A ATOM 1963 CG1 VAL A 261 −5.339 −9.236 10.954 1.00 24.43 AATOM 1964 CG2 VAL A 261 −4.526 −7.728 12.759 1.00 23.17 A ATOM 1965 CVAL A 261 −7.748 −7.640 10.645 1.00 21.55 A ATOM 1966 O VAL A 261 −8.525−8.473 11.109 1.00 20.82 A ATOM 1967 N ARG A 262 −7.880 −7.126 9.4281.00 21.55 A ATOM 1968 CA ARG A 262 −8.982 −7.514 8.564 1.00 22.38 AATOM 1969 CB ARG A 262 −9.961 −6.344 8.452 1.00 21.69 A ATOM 1970 CG ARGA 262 −10.631 −5.983 9.766 1.00 21.51 A ATOM 1971 CD ARG A 262 −11.517−7.128 10.288 1.00 22.91 A ATOM 1972 NE ARG A 262 −12.241 −6.748 11.5011.00 23.25 A ATOM 1973 CZ ARG A 262 −11.766 −6.836 12.740 1.00 24.30 AATOM 1974 NH1 ARG A 262 −10.547 −7.315 12.972 1.00 21.08 A ATOM 1975 NH2ARG A 262 −12.502 −6.398 13.753 1.00 24.59 A ATOM 1976 C ARG A 262−8.555 −7.997 7.178 1.00 22.47 A ATOM 1977 O ARG A 262 −7.366 −8.0196.852 1.00 22.56 A ATOM 1978 N GLU A 263 −9.525 −8.392 6.364 1.00 21.88A ATOM 1979 CA GLU A 263 −9.207 −8.888 5.035 1.00 22.36 A ATOM 1980 CBGLU A 263 −10.481 −9.388 4.355 1.00 22.82 A ATOM 1981 CG GLU A 263−11.010 −10.653 5.037 1.00 28.67 A ATOM 1982 CD GLU A 263 −12.505−10.893 4.844 1.00 33.40 A ATOM 1983 OE1 GLU A 263 −13.067 −11.739 5.5771.00 32.78 A ATOM 1984 OE2 GLU A 263 −13.120 −10.249 3.961 1.00 37.42 AATOM 1985 C GLU A 263 −8.486 −7.831 4.203 1.00 22.25 A ATOM 1986 O GLU A263 −7.881 −8.145 3.173 1.00 18.80 A ATOM 1987 N VAL A 264 −8.530 −6.5794.661 1.00 21.62 A ATOM 1988 CA VAL A 264 −7.835 −5.508 3.955 1.00 21.09A ATOM 1989 CB VAL A 264 −8.650 −4.211 3.935 1.00 22.68 A ATOM 1990 CG1VAL A 264 −9.941 −4.419 3.158 1.00 23.99 A ATOM 1991 CG2 VAL A 264−8.929 −3.758 5.355 1.00 21.59 A ATOM 1992 C VAL A 264 −6.500 −5.2224.630 1.00 20.86 A ATOM 1993 O VAL A 264 −5.816 −4.249 4.292 1.00 19.04A ATOM 1994 N GLY A 265 −6.135 −6.077 5.583 1.00 20.38 A ATOM 1995 CAGLY A 265 −4.896 −5.897 6.314 1.00 22.57 A ATOM 1996 C GLY A 265 −5.141−5.198 7.641 1.00 24.13 A ATOM 1997 O GLY A 265 −6.258 −5.210 8.154 1.0024.25 A ATOM 1998 N LEU A 266 −4.109 −4.575 8.195 1.00 24.55 A ATOM 1999CA LEU A 266 −4.257 −3.900 9.476 1.00 27.01 A ATOM 2000 CB LEU A 266−2.935 −3.923 10.259 1.00 26.32 A ATOM 2001 CG LEU A 266 −2.987 −4.17211.779 1.00 28.57 A ATOM 2002 CD1 LEU A 266 −1.872 −3.374 12.425 1.0025.69 A ATOM 2003 CD2 LEU A 266 −4.335 −3.764 12.389 1.00 25.63 A ATOM2004 C LEU A 266 −4.712 −2.457 9.301 1.00 28.29 A ATOM 2005 O LEU A 266−3.964 −1.618 8.809 1.00 27.00 A ATOM 2006 N THR A 267 −5.951 −2.1829.689 1.00 29.50 A ATOM 2007 CA THR A 267 −6.485 −.836 9.608 1.00 30.44A ATOM 2008 CB THR A 267 −8.022 −.825 9.574 1.00 29.41 A ATOM 2009 OG1THR A 267 −8.541 −1.701 10.579 1.00 28.88 A ATOM 2010 CG2 THR A 267−8.512 −1.271 8.220 1.00 31.59 A ATOM 2011 C THR A 267 −5.990 −.14310.861 1.00 32.37 A ATOM 2012 O THR A 267 −5.475 −.790 11.762 1.00 32.42A ATOM 2013 N PHE A 268 −6.153 1.168 10.931 1.00 34.52 A ATOM 2014 CAPHE A 268 −5.646 1.909 12.076 1.00 37.28 A ATOM 2015 CB PHE A 268 −4.2082.318 11.770 1.00 35.84 A ATOM 2016 CG PHE A 268 −3.713 3.443 12.5951.00 36.17 A ATOM 2017 CD1 PHE A 268 −3.373 3.249 13.927 1.00 38.58 AATOM 2018 CD2 PHE A 268 −3.576 4.709 12.039 1.00 36.83 A ATOM 2019 CE1PHE A 268 −2.895 4.309 14.700 1.00 39.39 A ATOM 2020 CE2 PHE A 268−3.104 5.771 12.798 1.00 37.60 A ATOM 2021 CZ PHE A 268 −2.762 5.57314.129 1.00 38.49 A ATOM 2022 C PHE A 268 −6.479 3.137 12.430 1.00 38.24A ATOM 2023 O PHE A 268 −6.645 4.041 11.613 1.00 38.90 A ATOM 2024 N GLNA 269 −7.000 3.157 13.655 1.00 39.85 A ATOM 2025 CA GLN A 269 −7.8054.274 14.138 1.00 40.66 A ATOM 2026 CB GLN A 269 −9.084 3.760 14.8151.00 40.42 A ATOM 2027 CG GLN A 269 −8.836 2.678 15.859 1.00 43.55 AATOM 2028 CD GLN A 269 −8.868 1.271 15.277 1.00 45.56 A ATOM 2029 OE1GLN A 269 −8.456 1.043 14.135 1.00 43.46 A ATOM 2030 NE2 GLN A 269−9.349 .316 16.069 1.00 44.36 A ATOM 2031 C GLN A 269 −6.957 5.06815.130 1.00 41.21 A ATOM 2032 O GLN A 269 −6.235 4.482 15.938 1.00 41.66A ATOM 2033 N LEU A 270 −7.041 6.396 15.061 1.00 41.43 A ATOM 2034 CALEU A 270 −6.263 7.264 15.944 1.00 41.35 A ATOM 2035 CB LEU A 270 −4.9277.598 15.273 1.00 40.81 A ATOM 2036 CG LEU A 270 −3.927 8.500 15.9911.00 42.32 A ATOM 2037 CD1 LEU A 270 −3.581 7.908 17.338 1.00 43.04 AATOM 2038 CD2 LEU A 270 −2.675 8.642 15.142 1.00 41.53 A ATOM 2039 C LEUA 270 −7.007 8.555 16.283 1.00 41.06 A ATOM 2040 O LEU A 270 −6.8819.554 15.575 1.00 44.11 A ATOM 2041 N LYS A 271 −7.786 8.540 17.358 1.0038.77 A ATOM 2042 CA LYS A 271 −8.537 9.730 17.762 1.00 37.60 A ATOM2043 CB LYS A 271 −9.392 9.420 18.999 1.00 36.95 A ATOM 2044 CG LYS A271 −10.504 8.407 18.714 1.00 38.43 A ATOM 2045 CD LYS A 271 −11.3378.048 19.940 1.00 37.75 A ATOM 2046 CE LYS A 271 −12.440 7.055 19.5551.00 40.27 A ATOM 2047 NZ LYS A 271 −13.165 6.457 20.723 1.00 42.36 AATOM 2048 C LYS A 271 −7.577 10.888 18.053 1.00 35.81 A ATOM 2049 O LYSA 271 −6.477 10.682 18.557 1.00 34.82 A ATOM 2050 N GLY A 272 −7.99812.105 17.724 1.00 34.36 A ATOM 2051 CA GLY A 272 −7.159 13.269 17.9551.00 32.41 A ATOM 2052 C GLY A 272 −6.859 13.596 19.412 1.00 31.39 AATOM 2053 O GLY A 272 −5.909 14.324 19.701 1.00 30.50 A ATOM 2054 N ALAA 273 −7.646 13.053 20.335 1.00 30.16 A ATOM 2055 CA ALA A 273 −7.44213.316 21.758 1.00 30.25 A ATOM 2056 CB ALA A 273 −8.680 12.896 22.5271.00 28.04 A ATOM 2057 C ALA A 273 −6.193 12.667 22.391 1.00 30.52 AATOM 2058 O ALA A 273 −5.906 12.886 23.572 1.00 31.69 A ATOM 2059 N VALA 274 −5.449 11.888 21.613 1.00 29.09 A ATOM 2060 CA VAL A 274 −4.25511.197 22.124 1.00 30.02 A ATOM 2061 CB VAL A 274 −3.574 10.349 20.9941.00 29.02 A ATOM 2062 CG1 VAL A 274 −2.120 10.066 21.328 1.00 26.26 AATOM 2063 CG2 VAL A 274 −4.324 9.029 20.829 1.00 28.14 A ATOM 2064 C VALA 274 −3.185 12.040 22.832 1.00 29.91 A ATOM 2065 O VAL A 274 −2.70611.667 23.908 1.00 31.11 A ATOM 2066 N PRO A 275 −2.785 13.174 22.2461.00 29.31 A ATOM 2067 CD PRO A 275 −3.039 13.717 20.903 1.00 28.93 AATOM 2068 CA PRO A 275 −1.759 13.959 22.943 1.00 29.97 A ATOM 2069 CBPRO A 275 −1.536 15.141 22.009 1.00 29.08 A ATOM 2070 CG PRO A 275−1.794 14.543 20.662 1.00 30.30 A ATOM 2071 C PRO A 275 −2.170 14.39124.348 1.00 30.48 A ATOM 2072 O PRO A 275 −1.355 14.376 25.271 1.0031.35 A ATOM 2073 N ASP A 276 −3.439 14.752 24.514 1.00 31.00 A ATOM2074 CA ASP A 276 −3.931 15.197 25.810 1.00 31.59 A ATOM 2075 CB ASP A276 −5.286 15.885 25.661 1.00 34.05 A ATOM 2076 CG ASP A 276 −5.84916.327 26.993 1.00 35.35 A ATOM 2077 OD1 ASP A 276 −5.196 17.162 27.6581.00 36.13 A ATOM 2078 OD2 ASP A 276 −6.927 15.829 27.384 1.00 36.47 AATOM 2079 C ASP A 276 −4.060 14.089 26.838 1.00 31.20 A ATOM 2080 O ASPA 276 −3.790 14.299 28.016 1.00 31.91 A ATOM 2081 N LEU A 277 −4.49212.913 26.400 1.00 32.16 A ATOM 2082 CA LEU A 277 −4.646 11.777 27.3031.00 31.43 A ATOM 2083 CB LEU A 277 −5.261 10.598 26.547 1.00 30.50 AATOM 2084 CG LEU A 277 −6.689 10.892 26.089 1.00 30.10 A ATOM 2085 CD1LEU A 277 −7.184 9.828 25.132 1.00 30.66 A ATOM 2086 CD2 LEU A 277−7.582 10.971 27.310 1.00 30.85 A ATOM 2087 C LEU A 277 −3.298 11.38127.903 1.00 31.68 A ATOM 2088 O LEU A 277 −3.166 11.214 29.114 1.0031.00 A ATOM 2089 N ILE A 278 −2.294 11.243 27.048 1.00 32.33 A ATOM2090 CA ILE A 278 −.962 10.887 27.502 1.00 32.96 A ATOM 2091 CB ILE A278 −.013 10.649 26.300 1.00 30.68 A ATOM 2092 CG2 ILE A 278 1.42210.523 26.777 1.00 28.01 A ATOM 2093 CG1 ILE A 278 −.456 9.391 25.5471.00 29.23 A ATOM 2094 CD1 ILE A 278 .283 9.139 24.250 1.00 29.89 A ATOM2095 C ILE A 278 −.378 11.966 28.406 1.00 34.32 A ATOM 2096 O ILE A 278.168 11.657 29.455 1.00 34.80 A ATOM 2097 N SER A 279 −.517 13.22928.011 1.00 36.66 A ATOM 2098 CA SER A 279 .025 14.351 28.790 1.00 37.98A ATOM 2099 CB SER A 279 −.114 15.663 28.002 1.00 40.15 A ATOM 2100 OGSER A 279 .917 15.792 27.031 1.00 41.42 A ATOM 2101 C SER A 279 −.55014.562 30.186 1.00 37.84 A ATOM 2102 O SER A 279 .193 14.762 31.151 1.0038.76 A ATOM 2103 N ALA A 280 −1.870 14.527 30.294 1.00 36.55 A ATOM2104 CA ALA A 280 −2.530 14.749 31.572 1.00 34.53 A ATOM 2105 CB ALA A280 −3.977 15.142 31.335 1.00 34.08 A ATOM 2106 C ALA A 280 −2.47113.547 32.490 1.00 35.22 A ATOM 2107 O ALA A 280 −3.258 13.450 33.4321.00 35.65 A ATOM 2108 N ASN A 281 −1.551 12.626 32.220 1.00 34.56 AATOM 2109 CA ASN A 281 −1.418 11.437 33.045 1.00 33.77 A ATOM 2110 CBASN A 281 −2.257 10.309 32.459 1.00 35.68 A ATOM 2111 CG ASN A 281−3.730 10.602 32.520 1.00 36.67 A ATOM 2112 OD1 ASN A 281 −4.386 10.34733.529 1.00 37.02 A ATOM 2113 ND2 ASN A 281 −4.258 11.169 31.447 1.0037.77 A ATOM 2114 C ASN A 281 .017 10.963 33.187 1.00 34.57 A ATOM 2115O ASN A 281 .323 10.141 34.057 1.00 33.59 A ATOM 2116 N ILE A 282 .90011.476 32.339 1.00 34.05 A ATOM 2117 CA ILE A 282 2.291 11.057 32.3831.00 36.36 A ATOM 2118 CB ILE A 282 3.060 11.550 31.128 1.00 36.30 AATOM 2119 CG2 ILE A 282 3.278 13.054 31.197 1.00 35.15 A ATOM 2120 CG1ILE A 282 4.388 10.803 31.010 1.00 36.39 A ATOM 2121 CD1 ILE A 282 5.06310.962 29.679 1.00 35.07 A ATOM 2122 C ILE A 282 2.976 11.540 33.6611.00 39.22 A ATOM 2123 O ILE A 282 3.876 10.874 34.183 1.00 40.83 A ATOM2124 N GLU A 283 2.534 12.687 34.172 1.00 38.71 A ATOM 2125 CA GLU A 2833.095 13.251 35.395 1.00 38.20 A ATOM 2126 CB GLU A 283 2.403 14.58635.710 1.00 39.81 A ATOM 2127 CG GLU A 283 2.918 15.313 36.936 1.0041.71 A ATOM 2128 CD GLU A 283 4.340 15.821 36.761 1.00 46.24 A ATOM2129 OE1 GLU A 283 4.717 16.782 37.472 1.00 45.68 A ATOM 2130 OE2 GLU A283 5.079 15.260 35.915 1.00 46.93 A ATOM 2131 C GLU A 283 2.868 12.26036.535 1.00 37.62 A ATOM 2132 O GLU A 283 3.760 11.988 37.340 1.00 37.84A ATOM 2133 N ASN A 284 1.654 11.726 36.579 1.00 37.45 A ATOM 2134 CAASN A 284 1.237 10.757 37.584 1.00 36.64 A ATOM 2135 CB ASN A 284 −.21110.353 37.300 1.00 38.10 A ATOM 2136 CG ASN A 284 −.766 9.388 38.3221.00 40.96 A ATOM 2137 OD1 ASN A 284 −1.919 8.971 38.219 1.00 43.35 AATOM 2138 ND2 ASN A 284 .042 9.028 39.316 1.00 41.64 A ATOM 2139 C ASN A284 2.138 9.522 37.567 1.00 36.15 A ATOM 2140 O ASN A 284 2.421 8.93238.606 1.00 34.35 A ATOM 2141 N CYS A 285 2.582 9.136 36.377 1.00 35.52A ATOM 2142 CA CYS A 285 3.449 7.977 36.232 1.00 37.87 A ATOM 2143 CBCYS A 285 3.511 7.556 34.764 1.00 39.05 A ATOM 2144 SG CYS A 285 1.9087.052 34.114 1.00 43.04 A ATOM 2145 C CYS A 285 4.858 8.242 36.761 1.0036.43 A ATOM 2146 O CYS A 285 5.515 7.339 37.268 1.00 36.47 A ATOM 2147N MET A 286 5.309 9.486 36.649 1.00 35.56 A ATOM 2148 CA MET A 286 6.6399.860 37.118 1.00 34.53 A ATOM 2149 CB MET A 286 7.033 11.227 36.5661.00 29.51 A ATOM 2150 CG MET A 286 7.148 11.285 35.060 1.00 27.11 AATOM 2151 SD MET A 286 8.518 10.331 34.419 1.00 17.52 A ATOM 2152 CE META 286 9.910 11.357 34.834 1.00 24.72 A ATOM 2153 C MET A 286 6.725 9.89238.641 1.00 34.62 A ATOM 2154 O MET A 286 7.770 9.561 39.206 1.00 34.71A ATOM 2155 N VAL A 287 5.639 10.292 39.305 1.00 34.59 A ATOM 2156 CAVAL A 287 5.648 10.352 40.764 1.00 34.53 A ATOM 2157 CB VAL A 287 4.55111.294 41.337 1.00 33.53 A ATOM 2158 CG1 VAL A 287 4.518 12.594 40.5511.00 32.05 A ATOM 2159 CG2 VAL A 287 3.198 10.602 41.339 1.00 33.56 AATOM 2160 C VAL A 287 5.448 8.964 41.348 1.00 36.11 A ATOM 2161 O VAL A287 5.612 8.764 42.551 1.00 38.82 A ATOM 2162 N GLU A 288 5.087 8.01140.490 1.00 37.10 A ATOM 2163 CA GLU A 288 4.879 6.630 40.912 1.00 36.49A ATOM 2164 CB GLU A 288 3.735 5.994 40.121 1.00 37.81 A ATOM 2165 CGGLU A 288 2.351 6.394 40.608 1.00 41.70 A ATOM 2166 CD GLU A 288 1.2465.589 39.945 1.00 43.46 A ATOM 2167 OE1 GLU A 288 .071 5.752 40.335 1.0042.08 A ATOM 2168 OE2 GLU A 288 1.555 4.791 39.032 1.00 45.61 A ATOM2169 C GLU A 288 6.154 5.812 40.724 1.00 34.02 A ATOM 2170 O GLU A 2886.383 4.826 41.417 1.00 35.06 A ATOM 2171 N ALA A 289 6.988 6.243 39.7921.00 32.31 A ATOM 2172 CA ALA A 289 8.229 5.553 39.504 1.00 34.35 A ATOM2173 CB ALA A 289 8.374 5.370 38.005 1.00 32.96 A ATOM 2174 C ALA A 2899.464 6.259 40.043 1.00 35.81 A ATOM 2175 O ALA A 289 10.570 5.74639.895 1.00 36.21 A ATOM 2176 N PHE A 290 9.303 7.422 40.672 1.00 37.04A ATOM 2177 CA PHE A 290 10.480 8.126 41.163 1.00 38.53 A ATOM 2178 CBPHE A 290 10.824 9.258 40.196 1.00 37.84 A ATOM 2179 CG PHE A 290 11.5108.785 38.945 1.00 37.15 A ATOM 2180 CD1 PHE A 290 12.854 8.420 38.9711.00 35.74 A ATOM 2181 CD2 PHE A 290 10.808 8.675 37.746 1.00 36.63 AATOM 2182 CE1 PHE A 290 13.488 7.950 37.822 1.00 35.20 A ATOM 2183 CE2PHE A 290 11.431 8.207 36.592 1.00 34.21 A ATOM 2184 CZ PHE A 290 12.7727.843 36.631 1.00 35.84 A ATOM 2185 C PHE A 290 10.510 8.643 42.600 1.0039.68 A ATOM 2186 O PHE A 290 11.593 8.932 43.129 1.00 38.64 A ATOM 2187N SER A 291 9.352 8.768 43.238 1.00 40.39 A ATOM 2188 CA SER A 291 9.3409.240 44.615 1.00 41.28 A ATOM 2189 CB SER A 291 7.902 9.336 45.138 1.0041.61 A ATOM 2190 OG SER A 291 7.321 8.052 45.305 1.00 42.21 A ATOM 2191C SER A 291 10.153 8.248 45.461 1.00 41.72 A ATOM 2192 O SER A 29110.838 8.634 46.411 1.00 41.43 A ATOM 2193 N GLN A 292 10.078 6.97045.088 1.00 41.71 A ATOM 2194 CA GLN A 292 10.798 5.899 45.776 1.0041.58 A ATOM 2195 CB GLN A 292 10.393 4.537 45.198 1.00 41.30 A ATOM2196 CG GLN A 292 10.805 4.334 43.744 1.00 43.26 A ATOM 2197 CD GLN A292 10.166 3.102 43.106 1.00 43.82 A ATOM 2198 OE1 GLN A 292 10.2421.992 43.644 1.00 44.70 A ATOM 2199 NE2 GLN A 292 9.538 3.295 41.9431.00 43.31 A ATOM 2200 C GLN A 292 12.312 6.090 45.642 1.00 41.07 A ATOM2201 O GLN A 292 13.095 5.469 46.365 1.00 40.68 A ATOM 2202 N PHE A 29312.717 6.944 44.708 1.00 40.42 A ATOM 2203 CA PHE A 293 14.129 7.23244.498 1.00 40.51 A ATOM 2204 CB PHE A 293 14.511 7.016 43.033 1.0039.74 A ATOM 2205 CG PHE A 293 14.218 5.639 42.543 1.00 39.95 A ATOM2206 CD1 PHE A 293 14.845 4.543 43.113 1.00 38.79 A ATOM 2207 CD2 PHE A293 13.273 5.429 41.548 1.00 40.76 A ATOM 2208 CE1 PHE A 293 14.5333.258 42.702 1.00 40.38 A ATOM 2209 CE2 PHE A 293 12.955 4.146 41.1311.00 38.84 A ATOM 2210 CZ PHE A 293 13.584 3.061 41.710 1.00 39.21 AATOM 2211 C PHE A 293 14.369 8.676 44.900 1.00 40.43 A ATOM 2212 O PHE A293 15.233 9.353 44.351 1.00 41.10 A ATOM 2213 N LYS A 294 13.589 9.12645.876 1.00 41.39 A ATOM 2214 CA LYS A 294 13.673 10.482 46.396 1.0042.03 A ATOM 2215 CB LYS A 294 14.806 10.593 47.425 1.00 42.52 A ATOM2216 CG LYS A 294 16.217 10.478 46.856 1.00 44.37 A ATOM 2217 CD LYS A294 17.124 11.572 47.438 1.00 46.80 A ATOM 2218 CE LYS A 294 18.46911.658 46.725 1.00 46.23 A ATOM 2219 NZ LYS A 294 19.268 12.839 47.1951.00 46.98 A ATOM 2220 C LYS A 294 13.893 11.502 45.285 1.00 42.25 AATOM 2221 O LYS A 294 14.693 12.423 45.435 1.00 42.94 A ATOM 2222 N ILEA 295 13.182 11.345 44.171 1.00 42.75 A ATOM 2223 CA ILE A 295 13.31812.281 43.058 1.00 43.31 A ATOM 2224 CB ILE A 295 13.915 11.616 41.8141.00 42.40 A ATOM 2225 CG2 ILE A 295 13.899 12.598 40.657 1.00 42.02 AATOM 2226 CG1 ILE A 295 15.351 11.165 42.092 1.00 42.85 A ATOM 2227 CD1ILE A 295 16.017 10.483 40.918 1.00 42.43 A ATOM 2228 C ILE A 295 11.99512.902 42.660 1.00 44.46 A ATOM 2229 O ILE A 295 11.004 12.201 42.4441.00 44.51 A ATOM 2230 N SER A 296 11.995 14.228 42.564 1.00 46.30 AATOM 2231 CA SER A 296 10.801 14.978 42.192 1.00 47.21 A ATOM 2232 CBSER A 296 10.308 15.827 43.369 1.00 48.70 A ATOM 2233 OG SER A 296 9.92115.012 44.463 1.00 52.02 A ATOM 2234 C SER A 296 11.048 15.877 40.9891.00 46.34 A ATOM 2235 O SER A 296 10.104 16.280 40.314 1.00 47.29 AATOM 2236 N ASP A 297 12.309 16.203 40.720 1.00 45.60 A ATOM 2237 CA ASPA 297 12.613 17.048 39.574 1.00 44.42 A ATOM 2238 CB ASP A 297 13.78517.981 39.878 1.00 46.17 A ATOM 2239 CG ASP A 297 14.192 18.825 38.6661.00 47.06 A ATOM 2240 OD1 ASP A 297 13.296 19.317 37.948 1.00 47.00 AATOM 2241 OD2 ASP A 297 15.407 19.000 38.436 1.00 47.36 A ATOM 2242 CASP A 297 12.920 16.219 38.329 1.00 44.32 A ATOM 2243 O ASP A 297 14.03615.727 38.135 1.00 44.05 A ATOM 2244 N TRP A 298 11.905 16.079 37.4881.00 42.80 A ATOM 2245 CA TRP A 298 12.001 15.327 36.253 1.00 40.26 AATOM 2246 CB TRP A 298 10.742 15.587 35.438 1.00 38.68 A ATOM 2247 CGTRP A 298 9.506 15.431 36.245 1.00 35.51 A ATOM 2248 CD2 TRP A 298 9.31314.553 37.363 1.00 35.36 A ATOM 2249 CE2 TRP A 298 7.985 14.735 37.8121.00 33.05 A ATOM 2250 CE3 TRP A 298 10.133 13.631 38.028 1.00 32.97 AATOM 2251 CD1 TRP A 298 8.326 16.087 36.065 1.00 36.11 A ATOM 2252 NE1TRP A 298 7.408 15.675 37.003 1.00 34.29 A ATOM 2253 CZ2 TRP A 298 7.45614.029 38.896 1.00 32.55 A ATOM 2254 CZ3 TRP A 298 9.607 12.929 39.1051.00 33.62 A ATOM 2255 CH2 TRP A 298 8.278 13.133 39.529 1.00 33.12 AATOM 2256 C TRP A 298 13.239 15.674 35.438 1.00 39.63 A ATOM 2257 O TRPA 298 13.873 14.797 34.862 1.00 36.85 A ATOM 2258 N ASN A 299 13.58416.956 35.399 1.00 40.40 A ATOM 2259 CA ASN A 299 14.744 17.401 34.6331.00 41.92 A ATOM 2260 CB ASN A 299 14.784 18.925 34.561 1.00 43.62 AATOM 2261 CG ASN A 299 13.930 19.460 33.447 1.00 46.32 A ATOM 2262 OD1ASN A 299 14.021 18.982 32.312 1.00 46.16 A ATOM 2263 ND2 ASN A 29913.094 20.456 33.752 1.00 45.79 A ATOM 2264 C ASN A 299 16.093 16.88935.119 1.00 41.44 A ATOM 2265 O ASN A 299 17.114 17.152 34.487 1.0041.03 A ATOM 2266 N LYS A 300 16.105 16.162 36.233 1.00 41.82 A ATOM2267 CA LYS A 300 17.355 15.615 36.753 1.00 40.46 A ATOM 2268 CB LYS A300 17.286 15.495 38.279 1.00 42.21 A ATOM 2269 CG LYS A 300 16.95016.803 38.973 1.00 42.69 A ATOM 2270 CD LYS A 300 17.123 16.740 40.4871.00 44.99 A ATOM 2271 CE LYS A 300 16.055 15.890 41.162 1.00 47.76 AATOM 2272 NZ LYS A 300 16.154 15.946 42.660 1.00 49.25 A ATOM 2273 C LYSA 300 17.583 14.237 36.121 1.00 38.83 A ATOM 2274 O LYS A 300 18.60113.581 36.370 1.00 38.08 A ATOM 2275 N LEU A 301 16.628 13.827 35.2851.00 36.04 A ATOM 2276 CA LEU A 301 16.647 12.531 34.601 1.00 34.97 AATOM 2277 CB LEU A 301 15.353 11.768 34.924 1.00 32.81 A ATOM 2278 CGLEU A 301 15.066 11.287 36.350 1.00 32.28 A ATOM 2279 CD1 LEU A 30115.321 12.393 37.346 1.00 34.57 A ATOM 2280 CD2 LEU A 301 13.619 10.85636.448 1.00 30.89 A ATOM 2281 C LEU A 301 16.766 12.645 33.078 1.0035.04 A ATOM 2282 O LEU A 301 16.238 13.590 32.484 1.00 36.33 A ATOM2283 N PHE A 302 17.460 11.697 32.439 1.00 34.85 A ATOM 2284 CA PHE A302 17.538 11.719 30.973 1.00 33.91 A ATOM 2285 CB PHE A 302 18.79611.008 30.441 1.00 33.60 A ATOM 2286 CG PHE A 302 18.885 9.555 30.7901.00 32.97 A ATOM 2287 CD1 PHE A 302 19.357 9.150 32.030 1.00 33.68 AATOM 2288 CD2 PHE A 302 18.534 8.585 29.855 1.00 34.78 A ATOM 2289 CE1PHE A 302 19.488 7.788 32.342 1.00 36.33 A ATOM 2290 CE2 PHE A 30218.657 7.221 30.151 1.00 36.72 A ATOM 2291 CZ PHE A 302 19.139 6.82231.402 1.00 36.20 A ATOM 2292 C PHE A 302 16.256 11.056 30.439 1.0032.30 A ATOM 2293 O PHE A 302 15.631 10.246 31.137 1.00 29.60 A ATOM2294 N TRP A 303 15.857 11.402 29.216 1.00 32.29 A ATOM 2295 CA TRP A303 14.607 10.881 28.660 1.00 31.71 A ATOM 2296 CB TRP A 303 13.63412.035 28.421 1.00 30.02 A ATOM 2297 CG TRP A 303 13.095 12.620 29.6621.00 31.30 A ATOM 2298 CD2 TRP A 303 11.745 12.559 30.113 1.00 31.48 AATOM 2299 CE2 TRP A 303 11.682 13.259 31.340 1.00 31.80 A ATOM 2300 CE3TRP A 303 10.579 11.981 29.602 1.00 32.51 A ATOM 2301 CD1 TRP A 30313.783 13.325 30.603 1.00 31.26 A ATOM 2302 NE1 TRP A 303 12.941 13.71431.617 1.00 31.13 A ATOM 2303 CZ2 TRP A 303 10.496 13.398 32.062 1.0031.38 A ATOM 2304 CZ3 TRP A 303 9.399 12.118 30.321 1.00 32.50 A ATOM2305 CH2 TRP A 303 9.368 12.823 31.538 1.00 32.74 A ATOM 2306 C TRP A303 14.581 10.016 27.413 1.00 30.99 A ATOM 2307 O TRP A 303 15.31110.233 26.460 1.00 30.40 A ATOM 2308 N VAL A 304 13.688 9.036 27.4431.00 31.60 A ATOM 2309 CA VAL A 304 13.469 8.151 26.313 1.00 31.46 AATOM 2310 CB VAL A 304 14.114 6.774 26.487 1.00 30.67 A ATOM 2311 CG1VAL A 304 13.707 5.886 25.324 1.00 28.82 A ATOM 2312 CG2 VAL A 30415.631 6.909 26.533 1.00 30.09 A ATOM 2313 C VAL A 304 11.970 7.96126.256 1.00 31.13 A ATOM 2314 O VAL A 304 11.416 7.160 27.002 1.00 32.32A ATOM 2315 N VAL A 305 11.318 8.713 25.377 1.00 30.86 A ATOM 2316 CAVAL A 305 9.869 8.656 25.224 1.00 30.15 A ATOM 2317 CB VAL A 305 9.24010.050 25.528 1.00 31.70 A ATOM 2318 CG1 VAL A 305 7.786 10.106 25.0431.00 30.98 A ATOM 2319 CG2 VAL A 305 9.308 10.322 27.028 1.00 30.26 AATOM 2320 C VAL A 305 9.516 8.220 23.805 1.00 29.92 A ATOM 2321 O VAL A305 10.157 8.637 22.840 1.00 29.78 A ATOM 2322 N HIS A 306 8.510 7.36323.679 1.00 29.35 A ATOM 2323 CA HIS A 306 8.105 6.899 22.360 1.00 30.96A ATOM 2324 CB HIS A 306 6.968 5.877 22.474 1.00 31.60 A ATOM 2325 CGHIS A 306 6.353 5.517 21.160 1.00 32.17 A ATOM 2326 CD2 HIS A 306 5.0995.701 20.683 1.00 31.92 A ATOM 2327 ND1 HIS A 306 7.063 4.907 20.1491.00 33.80 A ATOM 2328 CE1 HIS A 306 6.271 4.727 19.105 1.00 34.13 AATOM 2329 NE2 HIS A 306 5.074 5.201 19.404 1.00 32.34 A ATOM 2330 C HISA 306 7.672 8.087 21.487 1.00 30.79 A ATOM 2331 O HIS A 306 6.827 8.90921.881 1.00 30.02 A ATOM 2332 N PRO A 307 8.253 8.192 20.285 1.00 30.01A ATOM 2333 CD PRO A 307 9.351 7.348 19.777 1.00 29.05 A ATOM 2334 CAPRO A 307 7.946 9.272 19.346 1.00 29.75 A ATOM 2335 CB PRO A 307 9.1689.273 18.441 1.00 29.53 A ATOM 2336 CG PRO A 307 9.482 7.804 18.352 1.0028.95 A ATOM 2337 C PRO A 307 6.642 9.052 18.578 1.00 30.91 A ATOM 2338O PRO A 307 6.641 8.956 17.347 1.00 30.21 A ATOM 2339 N GLY A 308 5.5328.984 19.308 1.00 32.39 A ATOM 2340 CA GLY A 308 4.243 8.767 18.671 1.0034.41 A ATOM 2341 C GLY A 308 3.936 9.818 17.622 1.00 35.01 A ATOM 2342O GLY A 308 3.438 9.505 16.538 1.00 35.38 A ATOM 2343 N GLY A 309 4.24611.068 17.952 1.00 34.47 A ATOM 2344 CA GLY A 309 4.010 12.181 17.0461.00 32.80 A ATOM 2345 C GLY A 309 4.426 13.490 17.695 1.00 32.13 A ATOM2346 O GLY A 309 4.268 13.647 18.901 1.00 31.23 A ATOM 2347 N ARG A 3104.954 14.426 16.904 1.00 32.09 A ATOM 2348 CA ARG A 310 5.399 15.71717.424 1.00 33.38 A ATOM 2349 CB ARG A 310 5.408 16.791 16.323 1.0035.32 A ATOM 2350 CG ARG A 310 5.632 18.197 16.902 1.00 36.45 A ATOM2351 CD ARG A 310 5.225 19.329 15.976 1.00 38.46 A ATOM 2352 NE ARG A310 6.254 19.662 14.998 1.00 40.77 A ATOM 2353 CZ ARG A 310 6.164 20.68114.147 1.00 42.99 A ATOM 2354 NH1 ARG A 310 5.094 21.467 14.156 1.0044.81 A ATOM 2355 NH2 ARG A 310 7.138 20.918 13.280 1.00 44.76 A ATOM2356 C ARG A 310 4.536 16.227 18.576 1.00 33.42 A ATOM 2357 O ARG A 3105.048 16.539 19.653 1.00 32.55 A ATOM 2358 N ALA A 311 3.228 16.30118.330 1.00 34.76 A ATOM 2359 CA ALA A 311 2.251 16.787 19.304 1.0034.37 A ATOM 2360 CB ALA A 311 .842 16.595 18.766 1.00 34.77 A ATOM 2361C ALA A 311 2.383 16.133 20.666 1.00 35.11 A ATOM 2362 O ALA A 311 2.48816.832 21.673 1.00 36.46 A ATOM 2363 N ILE A 312 2.367 14.800 20.7051.00 34.41 A ATOM 2364 CA ILE A 312 2.514 14.079 21.971 1.00 33.63 AATOM 2365 CB ILE A 312 2.652 12.553 21.751 1.00 34.10 A ATOM 2366 CG2ILE A 312 3.117 11.869 23.044 1.00 31.59 A ATOM 2367 CG1 ILE A 312 1.31211.965 21.296 1.00 34.90 A ATOM 2368 CD1 ILE A 312 1.319 10.436 21.1751.00 32.76 A ATOM 2369 C ILE A 312 3.760 14.564 22.717 1.00 32.93 A ATOM2370 O ILE A 312 3.725 14.810 23.924 1.00 33.02 A ATOM 2371 N LEU A 3134.865 14.693 21.995 1.00 32.22 A ATOM 2372 CA LEU A 313 6.109 15.15222.602 1.00 32.28 A ATOM 2373 CB LEU A 313 7.268 14.982 21.615 1.0030.74 A ATOM 2374 CG LEU A 313 7.430 13.580 21.009 1.00 29.06 A ATOM2375 CD1 LEU A 313 8.656 13.542 20.117 1.00 27.85 A ATOM 2376 CD2 LEU A313 7.551 12.544 22.128 1.00 29.06 A ATOM 2377 C LEU A 313 5.988 16.61523.022 1.00 33.58 A ATOM 2378 O LEU A 313 6.449 17.002 24.095 1.00 31.21A ATOM 2379 N ASP A 314 5.352 17.428 22.185 1.00 34.88 A ATOM 2380 CAASP A 314 5.203 18.836 22.512 1.00 37.14 A ATOM 2381 CB ASP A 314 4.62319.620 21.335 1.00 36.64 A ATOM 2382 CG ASP A 314 5.573 19.681 20.1561.00 37.32 A ATOM 2383 OD1 ASP A 314 6.778 19.406 20.343 1.00 39.89 AATOM 2384 OD2 ASP A 314 5.123 20.013 19.039 1.00 38.32 A ATOM 2385 C ASPA 314 4.337 19.038 23.740 1.00 38.58 A ATOM 2386 O ASP A 314 4.61319.921 24.554 1.00 41.29 A ATOM 2387 N ARG A 315 3.298 18.226 23.8911.00 38.56 A ATOM 2388 CA ARG A 315 2.420 18.367 25.051 1.00 39.30 AATOM 2389 CB ARG A 315 1.076 17.661 24.801 1.00 39.89 A ATOM 2390 CG ARGA 315 −.038 18.094 25.756 1.00 41.38 A ATOM 2391 CD ARG A 315 −.53419.514 25.461 1.00 39.72 A ATOM 2392 NE ARG A 315 −1.525 19.517 24.3911.00 39.62 A ATOM 2393 CZ ARG A 315 −2.757 19.034 24.517 1.00 38.98 AATOM 2394 NH1 ARG A 315 −3.151 18.512 25.670 1.00 41.14 A ATOM 2395 NH2ARG A 315 −3.594 19.063 23.491 1.00 40.18 A ATOM 2396 C ARG A 315 3.09517.816 26.311 1.00 37.88 A ATOM 2397 O ARG A 315 3.120 18.474 27.3451.00 38.21 A ATOM 2398 N VAL A 316 3.650 16.614 26.220 1.00 38.10 A ATOM2399 CA VAL A 316 4.341 16.005 27.353 1.00 37.54 A ATOM 2400 CB VAL A316 5.071 14.695 26.932 1.00 38.03 A ATOM 2401 CG1 VAL A 316 6.07114.282 28.005 1.00 35.70 A ATOM 2402 CG2 VAL A 316 4.061 13.579 26.7131.00 36.09 A ATOM 2403 C VAL A 316 5.379 16.965 27.941 1.00 38.14 A ATOM2404 O VAL A 316 5.415 17.191 29.145 1.00 37.74 A ATOM 2405 N GLU A 3176.217 17.520 27.071 1.00 39.36 A ATOM 2406 CA GLU A 317 7.275 18.44427.462 1.00 40.74 A ATOM 2407 CB GLU A 317 8.078 18.846 26.227 1.0042.43 A ATOM 2408 CG GLU A 317 9.155 19.873 26.491 1.00 46.61 A ATOM2409 CD GLU A 317 10.033 20.092 25.280 1.00 49.20 A ATOM 2410 OE1 GLU A317 9.485 20.393 24.197 1.00 50.31 A ATOM 2411 OE2 GLU A 317 11.26919.959 25.409 1.00 51.28 A ATOM 2412 C GLU A 317 6.748 19.691 28.1611.00 40.41 A ATOM 2413 O GLU A 317 7.250 20.092 29.215 1.00 40.12 A ATOM2414 N ALA A 318 5.736 20.305 27.568 1.00 40.32 A ATOM 2415 CA ALA A 3185.148 21.502 28.140 1.00 40.04 A ATOM 2416 CB ALA A 318 4.103 22.06727.197 1.00 39.47 A ATOM 2417 C ALA A 318 4.517 21.164 29.482 1.00 40.63A ATOM 2418 O ALA A 318 4.609 21.938 30.436 1.00 40.11 A ATOM 2419 N LYSA 319 3.890 19.996 29.561 1.00 40.54 A ATOM 2420 CA LYS A 319 3.23619.585 30.793 1.00 43.33 A ATOM 2421 CB LYS A 319 2.442 18.294 30.5681.00 43.96 A ATOM 2422 CG LYS A 319 1.144 18.225 31.361 1.00 44.46 AATOM 2423 CD LYS A 319 1.434 18.187 32.849 1.00 45.75 A ATOM 2424 CE LYSA 319 .164 18.197 33.671 1.00 46.68 A ATOM 2425 NZ LYS A 319 .483 18.18235.128 1.00 48.59 A ATOM 2426 C LYS A 319 4.237 19.405 31.930 1.00 44.12A ATOM 2427 O LYS A 319 4.156 20.091 32.949 1.00 45.62 A ATOM 2428 N LEUA 320 5.186 18.493 31.757 1.00 44.99 A ATOM 2429 CA LEU A 320 6.20018.242 32.781 1.00 45.19 A ATOM 2430 CB LEU A 320 6.893 16.903 32.5211.00 43.92 A ATOM 2431 CG LEU A 320 6.180 15.639 33.016 1.00 43.85 AATOM 2432 CD1 LEU A 320 4.669 15.835 33.062 1.00 43.96 A ATOM 2433 CD2LEU A 320 6.550 14.490 32.106 1.00 41.61 A ATOM 2434 C LEU A 320 7.24319.346 32.848 1.00 45.43 A ATOM 2435 O LEU A 320 8.073 19.363 33.7521.00 47.16 A ATOM 2436 N ASN A 321 7.200 20.268 31.892 1.00 45.91 A ATOM2437 CA ASN A 321 8.156 21.371 31.857 1.00 46.17 A ATOM 2438 CB ASN A321 7.984 22.276 33.089 1.00 48.27 A ATOM 2439 CG ASN A 321 7.324 23.61332.757 1.00 50.11 A ATOM 2440 OD1 ASN A 321 7.887 24.431 32.016 1.0051.37 A ATOM 2441 ND2 ASN A 321 6.128 23.842 33.306 1.00 47.30 A ATOM2442 C ASN A 321 9.577 20.826 31.812 1.00 45.21 A ATOM 2443 O ASN A 32110.381 21.081 32.705 1.00 45.20 A ATOM 2444 N LEU A 322 9.875 20.06630.766 1.00 43.89 A ATOM 2445 CA LEU A 322 11.195 19.487 30.592 1.0043.18 A ATOM 2446 CB LEU A 322 11.094 18.173 29.817 1.00 42.20 A ATOM2447 CG LEU A 322 10.099 17.116 30.300 1.00 41.74 A ATOM 2448 CD1 LEU A322 10.180 15.896 29.386 1.00 40.69 A ATOM 2449 CD2 LEU A 322 10.39816.736 31.741 1.00 39.97 A ATOM 2450 C LEU A 322 12.082 20.455 29.8181.00 44.00 A ATOM 2451 O LEU A 322 11.597 21.240 29.002 1.00 45.63 AATOM 2452 N ASP A 323 13.381 20.405 30.077 1.00 44.78 A ATOM 2453 CA ASPA 323 14.317 21.265 29.369 1.00 47.10 A ATOM 2454 CB ASP A 323 15.71721.187 29.992 1.00 49.02 A ATOM 2455 CG ASP A 323 15.898 22.151 31.1471.00 51.43 A ATOM 2456 OD1 ASP A 323 15.816 23.377 30.911 1.00 52.39 AATOM 2457 OD2 ASP A 323 16.122 21.687 32.287 1.00 52.60 A ATOM 2458 CASP A 323 14.390 20.801 27.926 1.00 46.91 A ATOM 2459 O ASP A 323 14.44419.605 27.655 1.00 48.47 A ATOM 2460 N PRO A 324 14.396 21.743 26.9781.00 46.22 A ATOM 2461 CD PRO A 324 14.387 23.200 27.195 1.00 46.91 AATOM 2462 CA PRO A 324 14.465 21.436 25.550 1.00 46.06 A ATOM 2463 CBPRO A 324 14.791 22.787 24.930 1.00 45.50 A ATOM 2464 CG PRO A 32414.066 23.731 25.817 1.00 46.39 A ATOM 2465 C PRO A 324 15.525 20.39325.216 1.00 45.77 A ATOM 2466 O PRO A 324 15.591 19.916 24.086 1.0047.09 A ATOM 2467 N THR A 325 16.359 20.049 26.193 1.00 44.47 A ATOM2468 CA THR A 325 17.424 19.071 25.974 1.00 43.36 A ATOM 2469 CB THR A325 18.654 19.335 26.885 1.00 42.49 A ATOM 2470 OG1 THR A 325 18.31019.086 28.259 1.00 40.55 A ATOM 2471 CG2 THR A 325 19.144 20.768 26.7151.00 39.78 A ATOM 2472 C THR A 325 16.977 17.635 26.206 1.00 42.40 AATOM 2473 O THR A 325 17.518 16.716 25.607 1.00 43.43 A ATOM 2474 N LYSA 326 15.994 17.442 27.075 1.00 41.96 A ATOM 2475 CA LYS A 326 15.51016.104 27.369 1.00 41.14 A ATOM 2476 CB LYS A 326 14.252 16.172 28.2331.00 40.16 A ATOM 2477 CG LYS A 326 14.337 17.055 29.466 1.00 40.21 AATOM 2478 CD LYS A 326 15.143 16.444 30.595 1.00 42.29 A ATOM 2479 CELYS A 326 16.623 16.764 30.488 1.00 42.30 A ATOM 2480 NZ LYS A 32617.346 16.315 31.715 1.00 42.85 A ATOM 2481 C LYS A 326 15.197 15.31426.093 1.00 41.72 A ATOM 2482 O LYS A 326 15.702 14.205 25.902 1.0042.51 A ATOM 2483 N LEU A 327 14.381 15.893 25.214 1.00 42.21 A ATOM2484 CA LEU A 327 13.976 15.212 23.977 1.00 41.89 A ATOM 2485 CB LEU A327 12.533 15.590 23.617 1.00 40.14 A ATOM 2486 CG LEU A 327 11.47215.344 24.689 1.00 40.48 A ATOM 2487 CD1 LEU A 327 10.115 15.709 24.1241.00 40.17 A ATOM 2488 CD2 LEU A 327 11.491 13.888 25.138 1.00 40.61 AATOM 2489 C LEU A 327 14.854 15.410 22.740 1.00 41.12 A ATOM 2490 O LEUA 327 14.371 15.279 21.612 1.00 40.40 A ATOM 2491 N ILE A 328 16.12915.728 22.930 1.00 38.12 A ATOM 2492 CA ILE A 328 17.003 15.895 21.7801.00 36.92 A ATOM 2493 CB ILE A 328 18.380 16.460 22.183 1.00 36.66 AATOM 2494 CG2 ILE A 328 19.230 16.700 20.942 1.00 36.52 A ATOM 2495 CG1ILE A 328 18.199 17.772 22.945 1.00 36.61 A ATOM 2496 CD1 ILE A 32817.422 18.817 22.186 1.00 35.30 A ATOM 2497 C ILE A 328 17.174 14.50921.162 1.00 36.34 A ATOM 2498 O ILE A 328 17.106 14.343 19.939 1.0037.30 A ATOM 2499 N PRO A 329 17.396 13.488 22.003 1.00 34.69 A ATOM2500 CD PRO A 329 17.854 13.543 23.400 1.00 32.67 A ATOM 2501 CA PRO A329 17.559 12.135 21.462 1.00 35.34 A ATOM 2502 CB PRO A 329 17.97411.329 22.687 1.00 33.96 A ATOM 2503 CG PRO A 329 18.737 12.337 23.4911.00 33.23 A ATOM 2504 C PRO A 329 16.273 11.610 20.819 1.00 33.93 AATOM 2505 O PRO A 329 16.307 11.036 19.739 1.00 34.28 A ATOM 2506 N THRA 330 15.142 11.826 21.482 1.00 34.73 A ATOM 2507 CA THR A 330 13.84811.363 20.978 1.00 34.57 A ATOM 2508 CB THR A 330 12.718 11.627 22.0041.00 35.22 A ATOM 2509 OG1 THR A 330 12.959 10.873 23.200 1.00 36.60 AATOM 2510 CG2 THR A 330 11.376 11.209 21.430 1.00 36.40 A ATOM 2511 CTHR A 330 13.448 12.006 19.651 1.00 32.86 A ATOM 2512 O THR A 330 13.13311.309 18.685 1.00 32.91 A ATOM 2513 N ARG A 331 13.459 13.334 19.6141.00 32.31 A ATOM 2514 CA ARG A 331 13.088 14.081 18.418 1.00 31.64 AATOM 2515 CB ARG A 331 13.008 15.586 18.712 1.00 32.71 A ATOM 2516 CGARG A 331 11.900 16.012 19.676 1.00 31.50 A ATOM 2517 CD ARG A 33111.844 17.535 19.818 1.00 33.90 A ATOM 2518 NE ARG A 331 10.822 17.98120.761 1.00 33.69 A ATOM 2519 CZ ARG A 331 9.509 17.953 20.528 1.0037.09 A ATOM 2520 NH1 ARG A 331 9.031 17.506 19.373 1.00 36.82 A ATOM2521 NH2 ARG A 331 8.663 18.357 21.466 1.00 36.77 A ATOM 2522 C ARG A331 14.065 13.855 17.282 1.00 33.23 A ATOM 2523 O ARG A 331 13.69313.967 16.116 1.00 36.66 A ATOM 2524 N HIS A 332 15.314 13.540 17.6141.00 32.09 A ATOM 2525 CA HIS A 332 16.322 13.308 16.588 1.00 32.07 AATOM 2526 CB HIS A 332 17.720 13.310 17.210 1.00 35.42 A ATOM 2527 CGHIS A 332 18.796 12.893 16.258 1.00 38.11 A ATOM 2528 CD2 HIS A 33219.765 13.608 15.637 1.00 38.88 A ATOM 2529 ND1 HIS A 332 18.922 11.59715.800 1.00 38.66 A ATOM 2530 CE1 HIS A 332 19.921 11.534 14.938 1.0039.10 A ATOM 2531 NE2 HIS A 332 20.448 12.740 14.821 1.00 39.79 A ATOM2532 C HIS A 332 16.093 12.000 15.821 1.00 31.77 A ATOM 2533 O HIS A 33216.307 11.935 14.605 1.00 32.24 A ATOM 2534 N VAL A 333 15.677 10.95916.536 1.00 29.94 A ATOM 2535 CA VAL A 333 15.398 9.673 15.912 1.0028.63 A ATOM 2536 CB VAL A 333 15.344 8.544 16.975 1.00 29.30 A ATOM2537 CG1 VAL A 333 14.872 7.221 16.336 1.00 29.02 A ATOM 2538 CG2 VAL A333 16.731 8.371 17.602 1.00 24.24 A ATOM 2539 C VAL A 333 14.060 9.74715.156 1.00 28.45 A ATOM 2540 O VAL A 333 13.942 9.263 14.022 1.00 28.50A ATOM 2541 N MET A 334 13.055 10.363 15.768 1.00 26.42 A ATOM 2542 CAMET A 334 11.771 10.472 15.098 1.00 26.67 A ATOM 2543 CB MET A 33410.756 11.270 15.937 1.00 23.62 A ATOM 2544 CG MET A 334 9.286 11.00115.511 1.00 24.33 A ATOM 2545 SD MET A 334 8.068 12.270 15.942 1.0020.82 A ATOM 2546 CE MET A 334 7.430 11.702 17.373 1.00 19.41 A ATOM2547 C MET A 334 12.010 11.178 13.774 1.00 27.99 A ATOM 2548 O MET A 33411.385 10.851 12.767 1.00 29.09 A ATOM 2549 N SER A 335 12.937 12.13313.776 1.00 29.25 A ATOM 2550 CA SER A 335 13.241 12.888 12.568 1.0032.40 A ATOM 2551 CB SER A 335 14.107 14.104 12.888 1.00 31.79 A ATOM2552 OG SER A 335 14.464 14.759 11.683 1.00 32.15 A ATOM 2553 C SER A335 13.932 12.086 11.475 1.00 32.33 A ATOM 2554 O SER A 335 13.67612.296 10.288 1.00 34.30 A ATOM 2555 N GLU A 336 14.815 11.181 11.8711.00 32.37 A ATOM 2556 CA GLU A 336 15.535 10.372 10.901 1.00 31.39 AATOM 2557 CB GLU A 336 16.951 10.077 11.415 1.00 32.84 A ATOM 2558 CGGLU A 336 17.593 8.849 10.775 1.00 39.41 A ATOM 2559 CD GLU A 336 19.1038.788 10.950 1.00 42.04 A ATOM 2560 OE1 GLU A 336 19.606 9.199 12.0221.00 44.89 A ATOM 2561 OE2 GLU A 336 19.785 8.312 10.013 1.00 42.62 AATOM 2562 C GLU A 336 14.844 9.061 10.514 1.00 29.79 A ATOM 2563 O GLU A336 15.141 8.502 9.456 1.00 28.00 A ATOM 2564 N TYR A 337 13.914 8.58511.345 1.00 28.26 A ATOM 2565 CA TYR A 337 13.235 7.313 11.076 1.0027.55 A ATOM 2566 CB TYR A 337 13.656 6.273 12.118 1.00 25.68 A ATOM2567 CG TYR A 337 15.134 6.010 12.148 1.00 22.44 A ATOM 2568 CD1 TYR A337 15.719 5.099 11.272 1.00 21.51 A ATOM 2569 CE1 TYR A 337 17.1004.881 11.279 1.00 22.79 A ATOM 2570 CD2 TYR A 337 15.959 6.698 13.0311.00 21.39 A ATOM 2571 CE2 TYR A 337 17.336 6.489 13.046 1.00 23.04 AATOM 2572 CZ TYR A 337 17.896 5.579 12.170 1.00 22.73 A ATOM 2573 OH TYRA 337 19.244 5.356 12.205 1.00 25.92 A ATOM 2574 C TYR A 337 11.7147.351 11.047 1.00 28.12 A ATOM 2575 O TYR A 337 11.091 6.623 10.269 1.0029.61 A ATOM 2576 N GLY A 338 11.122 8.172 11.910 1.00 27.01 A ATOM 2577CA GLY A 338 9.674 8.261 11.985 1.00 28.08 A ATOM 2578 C GLY A 338 9.1717.349 13.095 1.00 29.03 A ATOM 2579 O GLY A 338 9.949 6.964 13.973 1.0030.16 A ATOM 2580 N ASN A 339 7.884 7.003 13.083 1.00 29.06 A ATOM 2581CA ASN A 339 7.364 6.111 14.112 1.00 28.44 A ATOM 2582 CB ASN A 3395.871 6.359 14.353 1.00 29.87 A ATOM 2583 CG ASN A 339 5.361 5.70215.643 1.00 32.77 A ATOM 2584 OD1 ASN A 339 5.898 4.682 16.094 1.0032.86 A ATOM 2585 ND2 ASN A 339 4.311 6.280 16.233 1.00 31.79 A ATOM2586 C ASN A 339 7.577 4.662 13.664 1.00 27.69 A ATOM 2587 O ASN A 3396.814 4.135 12.864 1.00 26.14 A ATOM 2588 N MET A 340 8.643 4.038 14.1561.00 28.00 A ATOM 2589 CA MET A 340 8.939 2.646 13.834 1.00 26.29 A ATOM2590 CB MET A 340 10.443 2.411 13.799 1.00 24.42 A ATOM 2591 CG MET A340 11.178 3.042 12.626 1.00 21.65 A ATOM 2592 SD MET A 340 12.917 2.67712.788 1.00 11.19 A ATOM 2593 CE MET A 340 13.287 3.727 14.106 1.0012.59 A ATOM 2594 C MET A 340 8.311 1.787 14.932 1.00 27.65 A ATOM 2595O MET A 340 8.795 .706 15.263 1.00 29.01 A ATOM 2596 N SER A 341 7.2192.300 15.487 1.00 28.65 A ATOM 2597 CA SER A 341 6.481 1.638 16.553 1.0028.94 A ATOM 2598 CB SER A 341 5.703 .440 16.001 1.00 30.35 A ATOM 2599OG SER A 341 4.905 −.161 17.013 1.00 33.28 A ATOM 2600 C SER A 341 7.3681.204 17.716 1.00 28.35 A ATOM 2601 O SER A 341 8.144 2.004 18.247 1.0027.65 A ATOM 2602 N SER A 342 7.253 −.067 18.097 1.00 28.96 A ATOM 2603CA SER A 342 7.997 −.622 19.222 1.00 29.52 A ATOM 2604 CB SER A 3427.624 −2.101 19.419 1.00 29.14 A ATOM 2605 OG SER A 342 7.844 −2.87318.249 1.00 28.82 A ATOM 2606 C SER A 342 9.516 −.474 19.197 1.00 30.70A ATOM 2607 O SER A 342 10.142 −.355 20.249 1.00 30.85 A ATOM 2608 N ALAA 343 10.118 −.464 18.016 1.00 31.45 A ATOM 2609 CA ALA A 343 11.570−.344 17.952 1.00 33.64 A ATOM 2610 CB ALA A 343 12.083 −.983 16.6621.00 35.55 A ATOM 2611 C ALA A 343 12.136 1.080 18.105 1.00 33.98 A ATOM2612 O ALA A 343 13.344 1.246 18.233 1.00 34.35 A ATOM 2613 N CYS A 34411.279 2.098 18.108 1.00 33.68 A ATOM 2614 CA CYS A 344 11.746 3.48418.244 1.00 33.68 A ATOM 2615 CB CYS A 344 10.566 4.455 18.206 1.0034.53 A ATOM 2616 SG CYS A 344 9.710 4.519 16.638 1.00 37.50 A ATOM 2617C CYS A 344 12.547 3.761 19.515 1.00 32.20 A ATOM 2618 O CYS A 34413.679 4.257 19.455 1.00 30.61 A ATOM 2619 N VAL A 345 11.953 3.43820.661 1.00 30.76 A ATOM 2620 CA VAL A 345 12.594 3.672 21.950 1.0030.62 A ATOM 2621 CB VAL A 345 11.700 3.227 23.104 1.00 30.70 A ATOM2622 CG1 VAL A 345 10.457 4.082 23.138 1.00 29.52 A ATOM 2623 CG2 VAL A345 11.339 1.764 22.939 1.00 29.04 A ATOM 2624 C VAL A 345 13.942 2.98422.091 1.00 30.41 A ATOM 2625 O VAL A 345 14.762 3.389 22.914 1.00 31.73A ATOM 2626 N HIS A 346 14.177 1.941 21.306 1.00 29.02 A ATOM 2627 CAHIS A 346 15.456 1.254 21.377 1.00 28.83 A ATOM 2628 CB HIS A 346 15.314−.201 20.924 1.00 29.96 A ATOM 2629 CG HIS A 346 14.336 −.983 21.7471.00 32.17 A ATOM 2630 CD2 HIS A 346 13.228 −1.681 21.400 1.00 32.87 AATOM 2631 ND1 HIS A 346 14.434 −1.083 23.118 1.00 33.79 A ATOM 2632 CE1HIS A 346 13.430 −1.809 23.580 1.00 34.75 A ATOM 2633 NE2 HIS A 34612.684 −2.186 22.557 1.00 34.86 A ATOM 2634 C HIS A 346 16.397 2.04520.486 1.00 28.71 A ATOM 2635 O HIS A 346 17.579 2.204 20.805 1.00 27.87A ATOM 2636 N PHE A 347 15.864 2.564 19.381 1.00 27.48 A ATOM 2637 CAPHE A 347 16.660 3.398 18.488 1.00 28.08 A ATOM 2638 CB PHE A 347 15.8203.906 17.314 1.00 25.80 A ATOM 2639 CG PHE A 347 15.953 3.083 16.0701.00 26.73 A ATOM 2640 CD1 PHE A 347 15.493 1.768 16.031 1.00 24.87 AATOM 2641 CD2 PHE A 347 16.539 3.621 14.927 1.00 24.25 A ATOM 2642 CE1PHE A 347 15.613 1.007 14.862 1.00 25.10 A ATOM 2643 CE2 PHE A 34716.666 2.863 13.758 1.00 23.84 A ATOM 2644 CZ PHE A 347 16.201 1.55813.727 1.00 25.46 A ATOM 2645 C PHE A 347 17.123 4.595 19.311 1.00 29.17A ATOM 2646 O PHE A 347 18.265 5.032 19.198 1.00 30.41 A ATOM 2647 N ILEA 348 16.220 5.115 20.144 1.00 29.54 A ATOM 2648 CA ILE A 348 16.5196.269 20.992 1.00 31.74 A ATOM 2649 CB ILE A 348 15.237 6.805 21.6701.00 30.12 A ATOM 2650 CG2 ILE A 348 15.585 7.905 22.673 1.00 29.86 AATOM 2651 CG1 ILE A 348 14.285 7.351 20.600 1.00 30.80 A ATOM 2652 CD1ILE A 348 12.905 7.697 21.121 1.00 29.48 A ATOM 2653 C ILE A 348 17.5645.941 22.057 1.00 33.22 A ATOM 2654 O ILE A 348 18.451 6.753 22.331 1.0032.42 A ATOM 2655 N LEU A 349 17.447 4.756 22.659 1.00 34.52 A ATOM 2656CA LEU A 349 18.402 4.312 23.673 1.00 33.45 A ATOM 2657 CB LEU A 34918.131 2.862 24.075 1.00 32.73 A ATOM 2658 CG LEU A 349 17.008 2.66325.082 1.00 31.86 A ATOM 2659 CD1 LEU A 349 16.621 1.218 25.144 1.0032.57 A ATOM 2660 CD2 LEU A 349 17.469 3.159 26.437 1.00 35.89 A ATOM2661 C LEU A 349 19.783 4.393 23.072 1.00 32.83 A ATOM 2662 O LEU A 34920.693 4.986 23.642 1.00 33.55 A ATOM 2663 N ASP A 350 19.912 3.79121.898 1.00 32.31 A ATOM 2664 CA ASP A 350 21.160 3.751 21.163 1.0032.68 A ATOM 2665 CB ASP A 350 20.953 2.948 19.883 1.00 31.76 A ATOM2666 CG ASP A 350 22.252 2.579 19.211 1.00 33.89 A ATOM 2667 OD1 ASP A350 23.090 1.926 19.866 1.00 34.37 A ATOM 2668 OD2 ASP A 350 22.4312.936 18.028 1.00 34.98 A ATOM 2669 C ASP A 350 21.662 5.162 20.836 1.0034.32 A ATOM 2670 O ASP A 350 22.793 5.513 21.161 1.00 33.23 A ATOM 2671N GLN A 351 20.820 5.971 20.202 1.00 35.14 A ATOM 2672 CA GLN A 35121.214 7.332 19.853 1.00 36.60 A ATOM 2673 CB GLN A 351 20.072 8.05219.134 1.00 37.06 A ATOM 2674 CG GLN A 351 20.442 9.464 18.680 1.0039.34 A ATOM 2675 CD GLN A 351 21.369 9.479 17.472 1.00 40.13 A ATOM2676 OE1 GLN A 351 22.018 10.480 17.198 1.00 40.84 A ATOM 2677 NE2 GLN A351 21.419 8.370 16.736 1.00 41.79 A ATOM 2678 C GLN A 351 21.617 8.12821.097 1.00 36.53 A ATOM 2679 O GLN A 351 22.511 8.977 21.039 1.00 34.64A ATOM 2680 N THR A 352 20.945 7.844 22.213 1.00 36.55 A ATOM 2681 CATHR A 352 21.219 8.507 23.481 1.00 37.35 A ATOM 2682 CB THR A 352 20.1438.164 24.523 1.00 36.83 A ATOM 2683 OG1 THR A 352 18.919 8.808 24.1591.00 36.13 A ATOM 2684 CG2 THR A 352 20.559 8.628 25.914 1.00 36.00 AATOM 2685 C THR A 352 22.600 8.137 24.032 1.00 39.55 A ATOM 2686 O THR A352 23.302 8.996 24.571 1.00 39.76 A ATOM 2687 N ARG A 353 22.995 6.87223.902 1.00 38.72 A ATOM 2688 CA ARG A 353 24.308 6.468 24.387 1.0039.16 A ATOM 2689 CB ARG A 353 24.395 4.949 24.547 1.00 38.70 A ATOM2690 CG ARG A 353 24.307 4.168 23.270 1.00 38.81 A ATOM 2691 CD ARG A353 24.503 2.685 23.524 1.00 38.69 A ATOM 2692 NE ARG A 353 24.489 1.93822.272 1.00 37.26 A ATOM 2693 CZ ARG A 353 24.949 .702 22.131 1.00 36.50A ATOM 2694 NH1 ARG A 353 25.463 .060 23.175 1.00 36.43 A ATOM 2695 NH2ARG A 353 24.910 .114 20.940 1.00 33.66 A ATOM 2696 C ARG A 353 25.4026.966 23.441 1.00 38.75 A ATOM 2697 O ARG A 353 26.491 7.322 23.889 1.0038.89 A ATOM 2698 N LYS A 354 25.110 6.999 22.140 1.00 38.70 A ATOM 2699CA LYS A 354 26.072 7.483 21.141 1.00 38.91 A ATOM 2700 CB LYS A 35425.530 7.291 19.716 1.00 39.12 A ATOM 2701 CG LYS A 354 25.177 5.87019.341 1.00 41.11 A ATOM 2702 CD LYS A 354 26.367 4.939 19.472 1.0041.53 A ATOM 2703 CE LYS A 354 25.948 3.481 19.275 1.00 43.16 A ATOM2704 NZ LYS A 354 25.334 3.220 17.934 1.00 42.80 A ATOM 2705 C LYS A 35426.345 8.981 21.355 1.00 39.02 A ATOM 2706 O LYS A 354 27.486 9.43821.281 1.00 39.72 A ATOM 2707 N ALA A 355 25.284 9.740 21.610 1.00 37.76A ATOM 2708 CA ALA A 355 25.403 11.168 21.827 1.00 37.38 A ATOM 2709 CBALA A 355 24.016 11.788 21.926 1.00 35.63 A ATOM 2710 C ALA A 355 26.21411.460 23.093 1.00 38.06 A ATOM 2711 O ALA A 355 27.016 12.392 23.1241.00 39.13 A ATOM 2712 N SER A 356 26.003 10.660 24.134 1.00 38.24 AATOM 2713 CA SER A 356 26.717 10.834 25.396 1.00 38.77 A ATOM 2714 CBSER A 356 26.194 9.849 26.448 1.00 39.74 A ATOM 2715 OG SER A 356 24.82810.086 26.754 1.00 40.96 A ATOM 2716 C SER A 356 28.200 10.579 25.1671.00 39.15 A ATOM 2717 O SER A 356 29.061 11.172 25.811 1.00 40.88 AATOM 2718 N LEU A 357 28.486 9.700 24.224 1.00 37.61 A ATOM 2719 CA LEUA 357 29.847 9.341 23.900 1.00 37.06 A ATOM 2720 CB LEU A 357 29.8138.048 23.096 1.00 34.46 A ATOM 2721 CG LEU A 357 31.079 7.221 22.9661.00 35.15 A ATOM 2722 CD1 LEU A 357 31.762 7.084 24.316 1.00 33.86 AATOM 2723 CD2 LEU A 357 30.701 5.861 22.387 1.00 35.10 A ATOM 2724 C LEUA 357 30.569 10.455 23.130 1.00 38.07 A ATOM 2725 O LEU A 357 31.62410.935 23.554 1.00 37.75 A ATOM 2726 N GLN A 358 29.992 10.860 22.0031.00 39.64 A ATOM 2727 CA GLN A 358 30.555 11.912 21.150 1.00 41.15 AATOM 2728 CB GLN A 358 29.603 12.218 19.987 1.00 43.94 A ATOM 2729 CGGLN A 358 29.325 11.065 19.026 1.00 46.51 A ATOM 2730 CD GLN A 35830.239 11.076 17.807 1.00 49.21 A ATOM 2731 OE1 GLN A 358 30.413 12.10917.150 1.00 50.20 A ATOM 2732 NE2 GLN A 358 30.817 9.923 17.491 1.0050.25 A ATOM 2733 C GLN A 358 30.807 13.213 21.901 1.00 41.73 A ATOM2734 O GLN A 358 31.811 13.894 21.676 1.00 41.83 A ATOM 2735 N ASN A 35929.885 13.557 22.792 1.00 41.97 A ATOM 2736 CA ASN A 359 29.978 14.79523.549 1.00 42.02 A ATOM 2737 CB ASN A 359 28.585 15.207 24.022 1.0042.01 A ATOM 2738 CG ASN A 359 27.546 15.082 22.924 1.00 42.17 A ATOM2739 OD1 ASN A 359 27.892 14.891 21.761 1.00 44.07 A ATOM 2740 ND2 ASN A359 26.269 15.186 23.285 1.00 42.37 A ATOM 2741 C ASN A 359 30.93014.721 24.728 1.00 43.88 A ATOM 2742 O ASN A 359 31.404 15.755 25.2081.00 45.52 A ATOM 2743 N GLY A 360 31.207 13.506 25.197 1.00 43.60 AATOM 2744 CA GLY A 360 32.118 13.332 26.320 1.00 41.65 A ATOM 2745 C GLYA 360 31.478 13.426 27.695 1.00 40.93 A ATOM 2746 O GLY A 360 32.09913.920 28.641 1.00 39.86 A ATOM 2747 N CYS A 361 30.244 12.938 27.8131.00 40.23 A ATOM 2748 CA CYS A 361 29.508 12.974 29.071 1.00 39.86 AATOM 2749 CB CYS A 361 28.021 12.710 28.816 1.00 41.39 A ATOM 2750 SGCYS A 361 27.254 13.841 27.604 1.00 46.32 A ATOM 2751 C CYS A 361 30.04311.968 30.083 1.00 39.25 A ATOM 2752 O CYS A 361 30.757 11.038 29.7301.00 39.13 A ATOM 2753 N SER A 362 29.680 12.163 31.344 1.00 39.05 AATOM 2754 CA SER A 362 30.128 11.303 32.428 1.00 38.13 A ATOM 2755 CBSER A 362 29.856 11.983 33.765 1.00 37.35 A ATOM 2756 OG SER A 36228.480 12.268 33.906 1.00 37.41 A ATOM 2757 C SER A 362 29.487 9.92032.432 1.00 39.61 A ATOM 2758 O SER A 362 30.080 8.962 32.926 1.00 39.97A ATOM 2759 N THR A 363 28.273 9.814 31.902 1.00 39.04 A ATOM 2760 CATHR A 363 27.582 8.527 31.864 1.00 38.14 A ATOM 2761 CB THR A 363 26.4828.449 32.943 1.00 38.58 A ATOM 2762 OG1 THR A 363 25.378 9.284 32.5691.00 34.35 A ATOM 2763 CG2 THR A 363 27.028 8.903 34.289 1.00 38.03 AATOM 2764 C THR A 363 26.928 8.299 30.507 1.00 37.71 A ATOM 2765 O THR A363 26.925 9.185 29.652 1.00 38.00 A ATOM 2766 N THR A 364 26.373 7.10730.312 1.00 36.07 A ATOM 2767 CA THR A 364 25.710 6.779 29.055 1.0034.36 A ATOM 2768 CB THR A 364 25.442 5.262 28.944 1.00 32.76 A ATOM2769 OG1 THR A 364 25.132 4.734 30.238 1.00 31.72 A ATOM 2770 CG2 THR A364 26.657 4.547 28.389 1.00 33.27 A ATOM 2771 C THR A 364 24.397 7.53928.917 1.00 34.89 A ATOM 2772 O THR A 364 23.788 7.552 27.855 1.00 33.55A ATOM 2773 N GLY A 365 23.971 8.174 30.001 1.00 37.02 A ATOM 2774 CAGLY A 365 22.738 8.939 29.985 1.00 39.62 A ATOM 2775 C GLY A 365 23.03110.424 29.873 1.00 41.66 A ATOM 2776 O GLY A 365 22.526 11.231 30.6551.00 41.20 A ATOM 2777 N GLU A 366 23.864 10.776 28.899 1.00 42.25 AATOM 2778 CA GLU A 366 24.248 12.161 28.660 1.00 44.72 A ATOM 2779 CBGLU A 366 23.085 12.903 27.996 1.00 47.19 A ATOM 2780 CG GLU A 36622.598 12.219 26.721 1.00 52.43 A ATOM 2781 CD GLU A 366 21.451 12.95026.035 1.00 56.02 A ATOM 2782 OE1 GLU A 366 20.404 13.181 26.686 1.0056.50 A ATOM 2783 OE2 GLU A 366 21.600 13.285 24.837 1.00 57.47 A ATOM2784 C GLU A 366 24.700 12.887 29.933 1.00 44.50 A ATOM 2785 O GLU A 36624.523 14.100 30.064 1.00 42.81 A ATOM 2786 N GLY A 367 25.279 12.13430.869 1.00 43.97 A ATOM 2787 CA GLY A 367 25.770 12.721 32.106 1.0042.81 A ATOM 2788 C GLY A 367 24.962 12.462 33.368 1.00 40.85 A ATOM2789 O GLY A 367 25.489 12.538 34.478 1.00 40.69 A ATOM 2790 N LEU A 36823.683 12.158 33.204 1.00 39.07 A ATOM 2791 CA LEU A 368 22.815 11.90434.340 1.00 37.27 A ATOM 2792 CB LEU A 368 21.374 12.223 33.947 1.0037.69 A ATOM 2793 CG LEU A 368 21.029 13.698 33.694 1.00 38.92 A ATOM2794 CD1 LEU A 368 22.240 14.489 33.220 1.00 38.52 A ATOM 2795 CD2 LEU A368 19.906 13.766 32.678 1.00 37.84 A ATOM 2796 C LEU A 368 22.94210.458 34.831 1.00 37.05 A ATOM 2797 O LEU A 368 23.465 9.590 34.1271.00 36.30 A ATOM 2798 N GLU A 369 22.458 10.206 36.041 1.00 36.23 AATOM 2799 CA GLU A 369 22.539 8.883 36.641 1.00 37.09 A ATOM 2800 CB GLUA 369 22.701 9.009 38.157 1.00 41.29 A ATOM 2801 CG GLU A 369 23.39810.294 38.642 1.00 46.01 A ATOM 2802 CD GLU A 369 22.517 11.551 38.5471.00 47.44 A ATOM 2803 OE1 GLU A 369 22.444 12.167 37.454 1.00 44.74 AATOM 2804 OE2 GLU A 369 21.894 11.914 39.578 1.00 49.56 A ATOM 2805 CGLU A 369 21.327 7.999 36.340 1.00 35.30 A ATOM 2806 O GLU A 369 21.4816.847 35.939 1.00 35.73 A ATOM 2807 N MET A 370 20.130 8.540 36.549 1.0032.75 A ATOM 2808 CA MET A 370 18.886 7.808 36.308 1.00 31.28 A ATOM2809 CB MET A 370 18.032 7.785 37.584 1.00 31.18 A ATOM 2810 CG MET A370 18.348 6.665 38.567 1.00 29.86 A ATOM 2811 SD MET A 370 17.143 6.65239.910 1.00 28.54 A ATOM 2812 CE MET A 370 17.895 7.805 40.972 1.0031.46 A ATOM 2813 C MET A 370 18.056 8.413 35.159 1.00 31.15 A ATOM 2814O MET A 370 18.125 9.615 34.893 1.00 29.39 A ATOM 2815 N GLY A 37117.268 7.574 34.491 1.00 28.64 A ATOM 2816 CA GLY A 371 16.449 8.05133.388 1.00 28.20 A ATOM 2817 C GLY A 371 15.117 7.328 33.246 1.00 26.64A ATOM 2818 O GLY A 371 14.882 6.297 33.879 1.00 24.42 A ATOM 2819 N VALA 372 14.236 7.861 32.408 1.00 25.98 A ATOM 2820 CA VAL A 372 12.9297.253 32.223 1.00 25.78 A ATOM 2821 CB VAL A 372 11.784 8.175 32.6951.00 25.32 A ATOM 2822 CG1 VAL A 372 11.584 9.324 31.708 1.00 24.95 AATOM 2823 CG2 VAL A 372 10.496 7.371 32.830 1.00 25.78 A ATOM 2824 C VALA 372 12.670 6.920 30.776 1.00 26.21 A ATOM 2825 O VAL A 372 13.1637.587 29.869 1.00 27.38 A ATOM 2826 N LEU A 373 11.892 5.873 30.566 1.0027.08 A ATOM 2827 CA LEU A 373 11.536 5.466 29.223 1.00 27.81 A ATOM2828 CB LEU A 373 12.218 4.149 28.866 1.00 29.56 A ATOM 2829 CG LEU A373 11.907 3.634 27.459 1.00 31.75 A ATOM 2830 CD1 LEU A 373 13.1713.065 26.836 1.00 29.26 A ATOM 2831 CD2 LEU A 373 10.791 2.591 27.5311.00 31.43 A ATOM 2832 C LEU A 373 10.026 5.317 29.194 1.00 27.20 A ATOM2833 O LEU A 373 9.427 4.811 30.148 1.00 26.34 A ATOM 2834 N PHE A 3749.418 5.779 28.106 1.00 26.82 A ATOM 2835 CA PHE A 374 7.972 5.71227.942 1.00 27.12 A ATOM 2836 CB PHE A 374 7.369 7.108 28.029 1.00 28.61A ATOM 2837 CG PHE A 374 7.242 7.630 29.421 1.00 31.11 A ATOM 2838 CD1PHE A 374 6.239 7.159 30.263 1.00 32.22 A ATOM 2839 CD2 PHE A 374 8.1108.609 29.891 1.00 31.24 A ATOM 2840 CE1 PHE A 374 6.093 7.655 31.5581.00 32.81 A ATOM 2841 CE2 PHE A 374 7.977 9.118 31.187 1.00 33.42 AATOM 2842 CZ PHE A 374 6.960 8.637 32.024 1.00 33.49 A ATOM 2843 C PHE A374 7.537 5.087 26.622 1.00 28.09 A ATOM 2844 O PHE A 374 8.186 5.24725.592 1.00 28.61 A ATOM 2845 N GLY A 375 6.423 4.370 26.671 1.00 27.67A ATOM 2846 CA GLY A 375 5.870 3.765 25.480 1.00 25.79 A ATOM 2847 C GLYA 375 4.377 4.025 25.530 1.00 25.72 A ATOM 2848 O GLY A 375 3.764 3.87826.583 1.00 26.86 A ATOM 2849 N PHE A 376 3.789 4.430 24.410 1.00 27.30A ATOM 2850 CA PHE A 376 2.349 4.694 24.363 1.00 26.31 A ATOM 2851 CBPHE A 376 2.061 6.168 24.072 1.00 27.66 A ATOM 2852 CG PHE A 376 2.9957.120 24.748 1.00 28.81 A ATOM 2853 CD1 PHE A 376 3.222 7.044 26.1151.00 30.56 A ATOM 2854 CD2 PHE A 376 3.628 8.117 24.019 1.00 28.26 AATOM 2855 CE1 PHE A 376 4.069 7.949 26.751 1.00 30.43 A ATOM 2856 CE2PHE A 376 4.475 9.026 24.643 1.00 29.11 A ATOM 2857 CZ PHE A 376 4.6988.943 26.011 1.00 29.04 A ATOM 2858 C PHE A 376 1.708 3.870 23.259 1.0025.27 A ATOM 2859 O PHE A 376 2.239 3.781 22.156 1.00 25.32 A ATOM 2860N GLY A 377 .555 3.284 23.552 1.00 25.39 A ATOM 2861 CA GLY A 377 −.1272.502 22.545 1.00 24.04 A ATOM 2862 C GLY A 377 −1.590 2.234 22.854 1.0023.88 A ATOM 2863 O GLY A 377 −2.155 2.812 23.785 1.00 20.92 A ATOM 2864N PRO A 378 −2.225 1.347 22.068 1.00 24.59 A ATOM 2865 CD PRO A 378−1.538 .702 20.934 1.00 22.15 A ATOM 2866 CA PRO A 378 −3.617 .90022.134 1.00 26.44 A ATOM 2867 CB PRO A 378 −3.608 −.340 21.259 1.0023.96 A ATOM 2868 CG PRO A 378 −2.682 .086 20.164 1.00 23.62 A ATOM 2869C PRO A 378 −4.134 .609 23.529 1.00 28.16 A ATOM 2870 O PRO A 378 −3.376.220 24.411 1.00 27.70 A ATOM 2871 N GLY A 379 −5.446 .775 23.690 1.0031.23 A ATOM 2872 CA GLY A 379 −6.111 .572 24.963 1.00 33.70 A ATOM 2873C GLY A 379 −5.864 1.875 25.669 1.00 36.78 A ATOM 2874 O GLY A 379−6.661 2.378 26.468 1.00 35.21 A ATOM 2875 N LEU A 380 −4.724 2.42125.259 1.00 38.76 A ATOM 2876 CA LEU A 380 −4.119 3.652 25.716 1.0037.20 A ATOM 2877 CB LEU A 380 −5.125 4.780 25.869 1.00 38.70 A ATOM2878 CG LEU A 380 −4.492 6.083 25.356 1.00 41.13 A ATOM 2879 CD1 LEU A380 −3.071 6.240 25.923 1.00 42.02 A ATOM 2880 CD2 LEU A 380 −4.4216.061 23.837 1.00 40.14 A ATOM 2881 C LEU A 380 −3.443 3.328 27.021 1.0034.99 A ATOM 2882 O LEU A 380 −3.848 3.763 28.098 1.00 34.48 A ATOM 2883N THR A 381 −2.406 2.514 26.893 1.00 31.04 A ATOM 2884 CA THR A 381−1.639 2.088 28.034 1.00 30.02 A ATOM 2885 CB THR A 381 −1.361 .54928.000 1.00 29.09 A ATOM 2886 OG1 THR A 381 −.002 .288 27.613 1.00 28.59A ATOM 2887 CG2 THR A 381 −2.282 −.117 27.011 1.00 26.08 A ATOM 2888 CTHR A 381 −.355 2.860 27.933 1.00 29.20 A ATOM 2889 O THR A 381 −.0253.380 26.874 1.00 29.92 A ATOM 2890 N ILE A 382 .358 2.951 29.042 1.0029.88 A ATOM 2891 CA ILE A 382 1.622 3.663 29.073 1.00 28.14 A ATOM 2892CB ILE A 382 1.520 4.957 29.914 1.00 26.61 A ATOM 2893 CG2 ILE A 3822.809 5.750 29.803 1.00 28.80 A ATOM 2894 CG1 ILE A 382 .324 5.80029.461 1.00 29.96 A ATOM 2895 CD1 ILE A 382 .455 6.415 28.079 1.00 29.52A ATOM 2896 C ILE A 382 2.607 2.729 29.759 1.00 27.30 A ATOM 2897 O ILEA 382 2.322 2.189 30.829 1.00 26.16 A ATOM 2898 N GLU A 383 3.747 2.50229.130 1.00 27.01 A ATOM 2899 CA GLU A 383 4.758 1.667 29.753 1.00 28.35A ATOM 2900 CB GLU A 383 5.385 .701 28.751 1.00 28.01 A ATOM 2901 CG GLUA 383 4.434 −.408 28.312 1.00 29.73 A ATOM 2902 CD GLU A 383 4.552−1.679 29.141 1.00 29.55 A ATOM 2903 OE1 GLU A 383 5.000 −1.623 30.3041.00 30.70 A ATOM 2904 OE2 GLU A 383 4.179 −2.748 28.626 1.00 31.96 AATOM 2905 C GLU A 383 5.792 2.644 30.261 1.00 28.17 A ATOM 2906 O GLU A383 6.263 3.496 29.523 1.00 28.48 A ATOM 2907 N THR A 384 6.098 2.53531.545 1.00 29.87 A ATOM 2908 CA THR A 384 7.083 3.379 32.192 1.00 29.87A ATOM 2909 CB THR A 384 6.516 4.060 33.458 1.00 31.48 A ATOM 2910 OG1THR A 384 5.424 4.922 33.099 1.00 35.27 A ATOM 2911 CG2 THR A 384 7.6174.869 34.160 1.00 29.36 A ATOM 2912 C THR A 384 8.240 2.496 32.620 1.0029.37 A ATOM 2913 O THR A 384 8.040 1.476 33.286 1.00 27.65 A ATOM 2914N VAL A 385 9.447 2.888 32.230 1.00 28.94 A ATOM 2915 CA VAL A 38510.632 2.137 32.603 1.00 28.87 A ATOM 2916 CB VAL A 385 11.220 1.38631.392 1.00 26.12 A ATOM 2917 CG1 VAL A 385 12.213 .339 31.862 1.0028.78 A ATOM 2918 CG2 VAL A 385 10.125 .744 30.601 1.00 25.84 A ATOM2919 C VAL A 385 11.702 3.074 33.177 1.00 30.37 A ATOM 2920 O VAL A 38512.218 3.957 32.475 1.00 31.40 A ATOM 2921 N VAL A 386 12.014 2.90034.461 1.00 31.00 A ATOM 2922 CA VAL A 386 13.044 3.709 35.104 1.0030.62 A ATOM 2923 CB VAL A 386 12.781 3.842 36.636 1.00 30.34 A ATOM2924 CG1 VAL A 386 12.562 2.499 37.232 1.00 31.84 A ATOM 2925 CG2 VAL A386 13.953 4.525 37.332 1.00 31.28 A ATOM 2926 C VAL A 386 14.377 3.01234.818 1.00 30.23 A ATOM 2927 O VAL A 386 14.593 1.855 35.190 1.00 30.15A ATOM 2928 N LEU A 387 15.254 3.725 34.120 1.00 30.35 A ATOM 2929 CALEU A 387 16.556 3.213 33.724 1.00 29.55 A ATOM 2930 CB LEU A 387 16.7873.490 32.244 1.00 27.05 A ATOM 2931 CG LEU A 387 15.906 2.768 31.2361.00 24.51 A ATOM 2932 CD1 LEU A 387 16.047 3.379 29.854 1.00 23.58 AATOM 2933 CD2 LEU A 387 16.310 1.333 31.215 1.00 23.31 A ATOM 2934 C LEUA 387 17.722 3.801 34.498 1.00 32.46 A ATOM 2935 O LEU A 387 17.7194.977 34.866 1.00 33.52 A ATOM 2936 N LYS A 388 18.726 2.965 34.724 1.0034.19 A ATOM 2937 CA LYS A 388 19.938 3.373 35.414 1.00 35.44 A ATOM2938 CB LYS A 388 20.313 2.348 36.483 1.00 37.24 A ATOM 2939 CG LYS A388 20.113 2.838 37.904 1.00 37.74 A ATOM 2940 CD LYS A 388 21.123 3.91038.251 1.00 37.39 A ATOM 2941 CE LYS A 388 22.518 3.331 38.292 1.0036.28 A ATOM 2942 NZ LYS A 388 22.602 2.295 39.339 1.00 37.97 A ATOM2943 C LYS A 388 21.056 3.445 34.379 1.00 37.08 A ATOM 2944 O LYS A 38821.298 2.484 33.633 1.00 36.42 A ATOM 2945 N SER A 389 21.726 4.59034.320 1.00 36.60 A ATOM 2946 CA SER A 389 22.825 4.769 33.387 1.0036.00 A ATOM 2947 CB SER A 389 23.022 6.259 33.114 1.00 37.01 A ATOM2948 OG SER A 389 24.013 6.455 32.130 1.00 38.47 A ATOM 2949 C SER A 38924.100 4.173 33.995 1.00 35.19 A ATOM 2950 O SER A 389 24.103 3.75335.152 1.00 32.14 A ATOM 2951 N VAL A 390 25.171 4.125 33.208 1.00 36.45A ATOM 2952 CA VAL A 390 26.465 3.617 33.677 1.00 38.33 A ATOM 2953 CBVAL A 390 26.885 2.274 32.987 1.00 39.52 A ATOM 2954 CG1 VAL A 39025.856 1.194 33.265 1.00 38.28 A ATOM 2955 CG2 VAL A 390 27.069 2.47331.481 1.00 38.97 A ATOM 2956 C VAL A 390 27.521 4.669 33.355 1.00 39.34A ATOM 2957 O VAL A 390 27.405 5.399 32.367 1.00 39.68 A ATOM 2958 N PROA 391 28.567 4.767 34.189 1.00 40.39 A ATOM 2959 CD PRO A 391 28.8364.016 35.428 1.00 39.55 A ATOM 2960 CA PRO A 391 29.614 5.759 33.9371.00 40.79 A ATOM 2961 CB PRO A 391 30.398 5.773 35.248 1.00 39.73 AATOM 2962 CG PRO A 391 30.282 4.369 35.712 1.00 39.36 A ATOM 2963 C PROA 391 30.473 5.395 32.736 1.00 42.01 A ATOM 2964 O PRO A 391 30.5634.223 32.354 1.00 42.53 A ATOM 2965 N ILE A 392 31.084 6.414 32.135 1.0043.00 A ATOM 2966 CA ILE A 392 31.949 6.240 30.978 1.00 43.81 A ATOM2967 CB ILE A 392 31.547 7.201 29.836 1.00 43.31 A ATOM 2968 CG2 ILE A392 32.465 7.006 28.631 1.00 43.26 A ATOM 2969 CG1 ILE A 392 30.1006.932 29.424 1.00 43.24 A ATOM 2970 CD1 ILE A 392 29.649 7.728 28.2241.00 43.15 A ATOM 2971 C ILE A 392 33.389 6.526 31.391 1.00 46.16 A ATOM2972 O ILE A 392 33.938 7.571 31.052 1.00 46.65 A ATOM 2973 N GLN A 39333.978 5.586 32.130 1.00 48.86 A ATOM 2974 CA GLN A 393 35.349 5.68332.631 1.00 52.16 A ATOM 2975 CB GLN A 393 35.644 7.096 33.149 1.0054.15 A ATOM 2976 CG GLN A 393 36.288 8.014 32.121 1.00 56.36 A ATOM2977 CD GLN A 393 37.683 7.566 31.722 1.00 57.85 A ATOM 2978 OE1 GLN A393 37.946 6.370 31.554 1.00 57.70 A ATOM 2979 NE2 GLN A 393 38.5858.529 31.553 1.00 58.57 A ATOM 2980 C GLN A 393 35.601 4.682 33.756 1.0053.17 A ATOM 2981 O GLN A 393 34.634 4.021 34.186 1.00 54.06 A ATOM 2982OXT GLN A 393 36.764 4.579 34.205 1.00 54.19 A

APPENDIX B Arachis hypogaea STS ATOM # TYPE RES X Y Z OCC B ATOM 1 CBVAL A 8 6.075 38.920 83.477 1.00 46.46 A ATOM 2 CG1 VAL A 8 5.638 40.11282.631 1.00 47.07 A ATOM 3 CG2 VAL A 8 6.142 37.664 82.618 1.00 46.26 AATOM 4 C VAL A 8 7.420 40.545 84.830 1.00 43.72 A ATOM 5 O VAL A 8 7.65641.588 84.215 1.00 43.86 A ATOM 6 N VAL A 8 7.847 38.099 85.052 1.0045.93 A ATOM 7 CA VAL A 8 7.460 39.195 84.117 1.00 45.01 A ATOM 8 N GLNA 9 7.122 40.527 86.125 1.00 40.46 A ATOM 9 CA GLN A 9 7.067 41.76386.892 1.00 36.43 A ATOM 10 CB GLN A 9 5.854 41.761 87.831 1.00 38.00 AATOM 11 CG GLN A 9 5.885 40.706 88.921 1.00 41.02 A ATOM 12 CD GLN A 94.619 40.706 89.764 1.00 43.48 A ATOM 13 OE1 GLN A 9 3.533 40.370 89.2831.00 43.47 A ATOM 14 NE2 GLN A 9 4.752 41.091 91.029 1.00 46.37 A ATOM15 C GLN A 9 8.354 41.972 87.688 1.00 32.96 A ATOM 16 O GLN A 9 8.50942.974 88.380 1.00 30.32 A ATOM 17 N ARG A 10 9.278 41.024 87.575 1.0029.75 A ATOM 18 CA ARG A 10 10.556 41.114 88.277 1.00 28.77 A ATOM 19 CBARG A 10 10.931 39.750 88.860 1.00 30.32 A ATOM 20 CG ARG A 10 11.25038.689 87.819 1.00 31.19 A ATOM 21 CD ARG A 10 11.006 37.297 88.382 1.0033.88 A ATOM 22 NE ARG A 10 11.685 37.098 89.662 1.00 34.38 A ATOM 23 CZARG A 10 11.524 36.031 90.441 1.00 35.70 A ATOM 24 NH1 ARG A 10 10.70035.053 90.078 1.00 34.56 A ATOM 25 NH2 ARG A 10 12.189 35.942 91.5871.00 30.48 A ATOM 26 C ARG A 10 11.643 41.582 87.314 1.00 27.02 A ATOM27 O ARG A 10 11.532 41.382 86.107 1.00 24.60 A ATOM 28 N ALA A 1112.686 42.215 87.848 1.00 24.89 A ATOM 29 CA ALA A 11 13.791 42.69287.023 1.00 23.28 A ATOM 30 CB ALA A 11 14.584 43.761 87.765 1.00 23.85A ATOM 31 C ALA A 11 14.689 41.510 86.674 1.00 24.68 A ATOM 32 O ALA A11 14.634 40.467 87.332 1.00 23.55 A ATOM 33 N GLU A 12 15.521 41.67485.649 1.00 24.82 A ATOM 34 CA GLU A 12 16.402 40.597 85.208 1.00 27.69A ATOM 35 CB GLU A 12 16.503 40.599 83.682 1.00 29.83 A ATOM 36 CG GLU A12 15.246 40.125 82.979 1.00 36.49 A ATOM 37 CD GLU A 12 14.809 38.74183.440 1.00 39.68 A ATOM 38 OE1 GLU A 12 14.131 38.637 84.489 1.00 42.41A ATOM 39 OE2 GLU A 12 15.155 37.754 82.756 1.00 42.52 A ATOM 40 C GLU A12 17.813 40.577 85.783 1.00 27.17 A ATOM 41 O GLU A 12 18.260 39.55386.306 1.00 28.17 A ATOM 42 N GLY A 13 18.515 41.699 85.673 1.00 23.56 AATOM 43 CA GLY A 13 19.887 41.758 86.147 1.00 22.50 A ATOM 44 C GLY A 1320.132 42.174 87.584 1.00 19.30 A ATOM 45 O GLY A 13 19.203 42.46988.335 1.00 18.70 A ATOM 46 N PRO A 14 21.402 42.203 87.997 1.00 17.89 AATOM 47 CD PRO A 14 22.595 41.786 87.239 1.00 19.36 A ATOM 48 CA PRO A14 21.751 42.591 89.366 1.00 17.15 A ATOM 49 CB PRO A 14 23.218 42.17789.475 1.00 18.61 A ATOM 50 CG PRO A 14 23.721 42.365 88.068 1.00 19.45A ATOM 51 C PRO A 14 21.546 44.085 89.615 1.00 15.71 A ATOM 52 O PRO A14 21.722 44.896 88.710 1.00 16.79 A ATOM 53 N ALA A 15 21.153 44.43390.837 1.00 13.60 A ATOM 54 CA ALA A 15 20.950 45.831 91.205 1.00 13.69A ATOM 55 CB ALA A 15 20.537 45.933 92.662 1.00 16.43 A ATOM 56 C ALA A15 22.270 46.562 90.973 1.00 14.74 A ATOM 57 O ALA A 15 23.349 46.06491.325 1.00 15.66 A ATOM 58 N THR A 16 22.181 47.748 90.391 1.00 14.49 AATOM 59 CA THR A 16 23.369 48.520 90.063 1.00 14.54 A ATOM 60 CB THR A16 23.540 48.550 88.540 1.00 16.93 A ATOM 61 OG1 THR A 16 23.544 47.20488.044 1.00 18.63 A ATOM 62 CG2 THR A 16 24.837 49.247 88.151 1.00 19.92A ATOM 63 C THR A 16 23.309 49.957 90.578 1.00 15.11 A ATOM 64 O THR A16 22.254 50.580 90.570 1.00 13.61 A ATOM 65 N VAL A 17 24.446 50.46891.039 1.00 14.91 A ATOM 66 CA VAL A 17 24.522 51.846 91.520 1.00 15.45A ATOM 67 CB VAL A 17 25.762 52.059 92.407 1.00 16.50 A ATOM 68 CG1 VALA 17 25.853 53.524 92.836 1.00 16.06 A ATOM 69 CG2 VAL A 17 25.68351.144 93.628 1.00 16.07 A ATOM 70 C VAL A 17 24.644 52.691 90.249 1.0014.23 A ATOM 71 O VAL A 17 25.572 52.499 89.462 1.00 14.44 A ATOM 72 NLEU A 18 23.701 53.606 90.052 1.00 13.45 A ATOM 73 CA LEU A 18 23.66554.443 88.857 1.00 14.26 A ATOM 74 CB LEU A 18 22.253 54.403 88.255 1.0015.14 A ATOM 75 CG LEU A 18 21.680 52.998 88.049 1.00 16.97 A ATOM 76CD1 LEU A 18 20.242 53.088 87.568 1.00 18.78 A ATOM 77 CD2 LEU A 1822.549 52.235 87.047 1.00 17.90 A ATOM 78 C LEU A 18 24.073 55.89889.076 1.00 14.73 A ATOM 79 O LEU A 18 24.351 56.613 88.120 1.00 14.38 AATOM 80 N ALA A 19 24.098 56.340 90.329 1.00 15.35 A ATOM 81 CA ALA A 1924.475 57.717 90.636 1.00 15.25 A ATOM 82 CB ALA A 19 23.388 58.68090.168 1.00 14.75 A ATOM 83 C ALA A 19 24.694 57.874 92.133 1.00 14.72 AATOM 84 O ALA A 19 24.086 57.166 92.942 1.00 14.23 A ATOM 85 N ILE A 2025.572 58.804 92.484 1.00 12.39 A ATOM 86 CA ILE A 20 25.891 59.09193.877 1.00 13.68 A ATOM 87 CB ILE A 20 27.221 58.442 94.304 1.00 14.33A ATOM 88 CG2 ILE A 20 27.465 58.691 95.795 1.00 14.65 A ATOM 89 CG1 ILEA 20 27.188 56.939 94.044 1.00 13.59 A ATOM 90 CD1 ILE A 20 28.53456.272 94.254 1.00 14.71 A ATOM 91 C ILE A 20 26.066 60.598 94.048 1.0013.50 A ATOM 92 O ILE A 20 26.766 61.231 93.260 1.00 15.34 A ATOM 93 NGLY A 21 25.433 61.152 95.075 1.00 14.62 A ATOM 94 CA GLY A 21 25.55462.571 95.373 1.00 14.32 A ATOM 95 C GLY A 21 25.774 62.738 96.872 1.0015.92 A ATOM 96 O GLY A 21 25.226 61.975 97.667 1.00 15.96 A ATOM 97 NTHR A 22 26.573 63.718 97.279 1.00 14.15 A ATOM 98 CA THR A 22 26.81663.918 98.703 1.00 13.46 A ATOM 99 CB THR A 22 28.236 63.435 99.115 1.0016.43 A ATOM 100 OG1 THR A 22 29.230 64.250 98.474 1.00 14.65 A ATOM 101CG2 THR A 22 28.450 61.966 98.705 1.00 14.38 A ATOM 102 C THR A 2226.677 65.382 99.094 1.00 13.65 A ATOM 103 O THR A 22 26.700 66.26798.239 1.00 13.92 A ATOM 104 N ALA A 23 26.555 65.625 100.394 1.00 12.89A ATOM 105 CA ALA A 23 26.417 66.981 100.911 1.00 13.53 A ATOM 106 CBALA A 23 24.999 67.467 100.696 1.00 13.62 A ATOM 107 C ALA A 23 26.75967.018 102.394 1.00 13.65 A ATOM 108 O ALA A 23 26.660 66.007 103.0901.00 12.16 A ATOM 109 N ASN A 24 27.171 68.186 102.879 1.00 13.77 A ATOM110 CA ASN A 24 27.510 68.348 104.291 1.00 12.71 A ATOM 111 CB ASN A 2429.010 68.177 104.559 1.00 15.73 A ATOM 112 CG ASN A 24 29.599 66.941103.929 1.00 16.23 A ATOM 113 OD1 ASN A 24 29.953 66.940 102.747 1.0016.19 A ATOM 114 ND2 ASN A 24 29.726 65.881 104.719 1.00 13.70 A ATOM115 C ASN A 24 27.199 69.776 104.702 1.00 15.49 A ATOM 116 O ASN A 2427.161 70.675 103.865 1.00 14.90 A ATOM 117 N PRO A 25 26.965 70.001105.998 1.00 17.07 A ATOM 118 CD PRO A 25 26.692 69.058 107.094 1.0016.81 A ATOM 119 CA PRO A 25 26.694 71.381 106.403 1.00 17.11 A ATOM 120CB PRO A 25 26.360 71.250 107.892 1.00 17.63 A ATOM 121 CG PRO A 2526.961 69.912 108.300 1.00 19.53 A ATOM 122 C PRO A 25 27.996 72.152106.118 1.00 20.50 A ATOM 123 O PRO A 25 29.087 71.580 106.161 1.0018.51 A ATOM 124 N PRO A 26 27.897 73.451 105.805 1.00 20.76 A ATOM 125CD PRO A 26 26.654 74.240 105.817 1.00 22.95 A ATOM 126 CA PRO A 2629.053 74.305 105.499 1.00 21.72 A ATOM 127 CB PRO A 26 28.399 75.619105.080 1.00 24.14 A ATOM 128 CG PRO A 26 27.176 75.660 105.947 1.0025.19 A ATOM 129 C PRO A 26 30.106 74.512 106.590 1.00 21.55 A ATOM 130O PRO A 26 31.299 74.601 106.296 1.00 23.48 A ATOM 131 N ASN A 27 29.67174.598 107.839 1.00 20.95 A ATOM 132 CA ASN A 27 30.589 74.813 108.9541.00 21.75 A ATOM 133 CB ASN A 27 29.788 74.956 110.245 1.00 20.97 AATOM 134 CG ASN A 27 30.650 75.307 111.433 1.00 22.82 A ATOM 135 OD1 ASNA 27 31.412 76.273 111.396 1.00 21.91 A ATOM 136 ND2 ASN A 27 30.52474.530 112.507 1.00 21.17 A ATOM 137 C ASN A 27 31.620 73.695 109.1081.00 21.96 A ATOM 138 O ASN A 27 31.258 72.544 109.367 1.00 21.55 A ATOM139 N CYS A 28 32.898 74.042 108.957 1.00 21.41 A ATOM 140 CA CYS A 2833.993 73.077 109.082 1.00 24.36 A ATOM 141 CB CYS A 28 34.957 73.194107.905 1.00 26.72 A ATOM 142 SG CYS A 28 34.296 72.622 106.349 1.0032.06 A ATOM 143 C CYS A 28 34.793 73.287 110.351 1.00 25.08 A ATOM 144O CYS A 28 35.100 74.422 110.713 1.00 26.06 A ATOM 145 N ILE A 29 35.14372.197 111.024 1.00 23.86 A ATOM 146 CA ILE A 29 35.940 72.317 112.2331.00 23.59 A ATOM 147 CB ILE A 29 35.266 71.650 113.451 1.00 26.59 AATOM 148 CG2 ILE A 29 33.906 72.300 113.715 1.00 26.52 A ATOM 149 CG1ILE A 29 35.128 70.148 113.215 1.00 27.45 A ATOM 150 CD1 ILE A 29 34.66469.387 114.434 1.00 32.28 A ATOM 151 C ILE A 29 37.322 71.711 112.0421.00 22.44 A ATOM 152 O ILE A 29 37.474 70.597 111.536 1.00 19.22 A ATOM153 N ASP A 30 38.334 72.476 112.435 1.00 21.63 A ATOM 154 CA ASP A 3039.718 72.044 112.340 1.00 21.62 A ATOM 155 CB ASP A 30 40.640 73.254112.432 1.00 25.37 A ATOM 156 CG ASP A 30 42.069 72.915 112.107 1.0026.61 A ATOM 157 OD1 ASP A 30 42.551 71.875 112.595 1.00 29.92 A ATOM158 OD2 ASP A 30 42.713 73.691 111.369 1.00 31.88 A ATOM 159 C ASP A 3039.978 71.105 113.517 1.00 20.05 A ATOM 160 O ASP A 30 39.899 71.513114.671 1.00 19.05 A ATOM 161 N GLN A 31 40.292 69.849 113.221 1.0020.36 A ATOM 162 CA GLN A 31 40.529 68.856 114.265 1.00 19.11 A ATOM 163CB GLN A 31 40.742 67.480 113.625 1.00 17.44 A ATOM 164 CG GLN A 3140.787 66.306 114.596 1.00 21.06 A ATOM 165 CD GLN A 31 39.430 65.957115.189 1.00 21.80 A ATOM 166 OE1 GLN A 31 39.207 64.826 115.619 1.0025.66 A ATOM 167 NE2 GLN A 31 38.525 66.926 115.230 1.00 18.69 A ATOM168 C GLN A 31 41.722 69.200 115.151 1.00 19.87 A ATOM 169 O GLN A 3141.703 68.931 116.348 1.00 18.46 A ATOM 170 N SER A 32 42.752 69.803114.564 1.00 20.70 A ATOM 171 CA SER A 32 43.956 70.157 115.311 1.0022.04 A ATOM 172 CB SER A 32 45.019 70.734 114.363 1.00 22.43 A ATOM 173OG SER A 32 44.665 72.032 113.906 1.00 24.69 A ATOM 174 C SER A 3243.694 71.143 116.453 1.00 22.19 A ATOM 175 O SER A 32 44.441 71.178117.429 1.00 22.11 A ATOM 176 N THR A 33 42.631 71.933 116.342 1.0021.38 A ATOM 177 CA THR A 33 42.308 72.911 117.379 1.00 20.69 A ATOM 178CB THR A 33 42.300 74.343 116.801 1.00 22.44 A ATOM 179 OG1 THR A 3341.251 74.459 115.834 1.00 22.63 A ATOM 180 CG2 THR A 33 43.635 74.664116.132 1.00 24.73 A ATOM 181 C THR A 33 40.943 72.663 118.028 1.0018.62 A ATOM 182 O THR A 33 40.438 73.515 118.754 1.00 18.50 A ATOM 183N TYR A 34 40.346 71.499 117.787 1.00 16.74 A ATOM 184 CA TYR A 3439.029 71.226 118.355 1.00 16.94 A ATOM 185 CB TYR A 34 38.451 69.928117.801 1.00 17.19 A ATOM 186 CG TYR A 34 36.975 69.790 118.083 1.0017.35 A ATOM 187 CD1 TYR A 34 36.058 70.685 117.526 1.00 17.15 A ATOM188 CE1 TYR A 34 34.693 70.575 117.788 1.00 19.47 A ATOM 189 CD2 TYR A34 36.491 68.780 118.911 1.00 16.08 A ATOM 190 CE2 TYR A 34 35.13368.661 119.183 1.00 17.26 A ATOM 191 CZ TYR A 34 34.237 69.562 118.6171.00 17.18 A ATOM 192 OH TYR A 34 32.891 69.457 118.893 1.00 16.72 AATOM 193 C TYR A 34 38.992 71.157 119.874 1.00 17.22 A ATOM 194 O TYR A34 38.015 71.583 120.490 1.00 18.03 A ATOM 195 N ALA A 35 40.043 70.604120.474 1.00 17.84 A ATOM 196 CA ALA A 35 40.107 70.489 121.926 1.0018.20 A ATOM 197 CB ALA A 35 41.448 69.913 122.355 1.00 18.99 A ATOM 198C ALA A 35 39.904 71.867 122.550 1.00 18.82 A ATOM 199 O ALA A 35 39.09172.028 123.448 1.00 17.85 A ATOM 200 N ASP A 36 40.653 72.858 122.0731.00 18.76 A ATOM 201 CA ASP A 36 40.516 74.213 122.604 1.00 19.92 AATOM 202 CB ASP A 36 41.438 75.190 121.864 1.00 22.24 A ATOM 203 CG ASPA 36 42.903 74.972 122.181 1.00 25.34 A ATOM 204 OD1 ASP A 36 43.21774.578 123.324 1.00 25.77 A ATOM 205 OD2 ASP A 36 43.745 75.213 121.2871.00 29.04 A ATOM 206 C ASP A 36 39.078 74.709 122.478 1.00 20.11 A ATOM207 O ASP A 36 38.477 75.179 123.452 1.00 19.46 A ATOM 208 N TYR A 3738.538 74.611 121.266 1.00 18.02 A ATOM 209 CA TYR A 37 37.180 75.057120.991 1.00 17.23 A ATOM 210 CB TYR A 37 36.846 74.817 119.514 1.0016.64 A ATOM 211 CG TYR A 37 35.399 75.092 119.152 1.00 19.58 A ATOM 212CD1 TYR A 37 34.945 76.396 118.946 1.00 19.88 A ATOM 213 CE1 TYR A 3733.615 76.654 118.611 1.00 21.95 A ATOM 214 CD2 TYR A 37 34.482 74.046119.020 1.00 18.32 A ATOM 215 CE2 TYR A 37 33.153 74.290 118.690 1.0021.26 A ATOM 216 CZ TYR A 37 32.725 75.598 118.483 1.00 22.45 A ATOM 217OH TYR A 37 31.417 75.846 118.136 1.00 22.04 A ATOM 218 C TYR A 3736.158 74.342 121.865 1.00 17.32 A ATOM 219 O TYR A 37 35.352 74.977122.553 1.00 17.84 A ATOM 220 N TYR A 38 36.198 73.013 121.829 1.0017.92 A ATOM 221 CA TYR A 38 35.270 72.178 122.585 1.00 17.56 A ATOM 222CB TYR A 38 35.626 70.702 122.369 1.00 16.77 A ATOM 223 CG TYR A 3834.755 69.726 123.116 1.00 16.04 A ATOM 224 CD1 TYR A 38 33.436 69.484122.724 1.00 17.14 A ATOM 225 CE1 TYR A 38 32.635 68.580 123.420 1.0017.33 A ATOM 226 CD2 TYR A 38 35.251 69.039 124.224 1.00 16.93 A ATOM227 CE2 TYR A 38 34.466 68.140 124.923 1.00 17.51 A ATOM 228 CZ TYR A 3833.161 67.913 124.519 1.00 16.76 A ATOM 229 OH TYR A 38 32.398 67.030125.234 1.00 17.13 A ATOM 230 C TYR A 38 35.248 72.506 124.076 1.0018.55 A ATOM 231 O TYR A 38 34.185 72.752 124.646 1.00 18.23 A ATOM 232N PHE A 39 36.412 72.517 124.714 1.00 19.37 A ATOM 233 CA PHE A 3936.453 72.813 126.143 1.00 19.56 A ATOM 234 CB PHE A 39 37.816 72.429126.722 1.00 19.04 A ATOM 235 CG PHE A 39 37.907 70.975 127.108 1.0020.13 A ATOM 236 CD1 PHE A 39 37.759 70.583 128.434 1.00 21.28 A ATOM237 CD2 PHE A 39 38.075 69.993 126.135 1.00 19.97 A ATOM 238 CE1 PHE A39 37.774 69.230 128.788 1.00 21.03 A ATOM 239 CE2 PHE A 39 38.09168.645 126.476 1.00 19.95 A ATOM 240 CZ PHE A 39 37.939 68.262 127.8061.00 21.19 A ATOM 241 C PHE A 39 36.086 74.255 126.485 1.00 20.19 A ATOM242 O PHE A 39 35.732 74.553 127.622 1.00 22.34 A ATOM 243 N ARG A 4036.144 75.143 125.499 1.00 20.54 A ATOM 244 CA ARG A 40 35.773 76.534125.734 1.00 20.65 A ATOM 245 CB ARG A 40 36.470 77.456 124.726 1.0019.69 A ATOM 246 CG ARG A 40 36.044 78.918 124.836 1.00 22.28 A ATOM 247CD ARG A 40 36.875 79.813 123.925 1.00 23.38 A ATOM 248 NE ARG A 4036.646 79.562 122.503 1.00 23.95 A ATOM 249 CZ ARG A 40 35.519 79.851121.861 1.00 24.46 A ATOM 250 NH1 ARG A 40 34.507 80.404 122.510 1.0025.71 A ATOM 251 NH2 ARG A 40 35.403 79.585 120.567 1.00 26.85 A ATOM252 C ARG A 40 34.257 76.707 125.627 1.00 20.55 A ATOM 253 O ARG A 4033.620 77.242 126.540 1.00 18.76 A ATOM 254 N VAL A 41 33.674 76.245124.522 1.00 20.21 A ATOM 255 CA VAL A 41 32.236 76.385 124.338 1.0021.46 A ATOM 256 CB VAL A 41 31.790 76.005 122.892 1.00 22.92 A ATOM 257CG1 VAL A 41 32.537 76.875 121.879 1.00 23.74 A ATOM 258 CG2 VAL A 4132.037 74.524 122.619 1.00 21.78 A ATOM 259 C VAL A 41 31.417 75.599125.350 1.00 21.29 A ATOM 260 O VAL A 41 30.261 75.928 125.588 1.0020.77 A ATOM 261 N THR A 42 32.001 74.562 125.949 1.00 21.64 A ATOM 262CA THR A 42 31.274 73.785 126.951 1.00 22.13 A ATOM 263 CB THR A 4231.532 72.254 126.828 1.00 21.03 A ATOM 264 OG1 THR A 42 32.914 71.968127.082 1.00 19.85 A ATOM 265 CG2 THR A 42 31.155 71.758 125.440 1.0018.84 A ATOM 266 C THR A 42 31.670 74.237 128.360 1.00 24.77 A ATOM 267O THR A 42 31.365 73.564 129.344 1.00 24.42 A ATOM 268 N ASN A 43 32.35775.375 128.442 1.00 25.63 A ATOM 269 CA ASN A 43 32.781 75.945 129.7221.00 27.73 A ATOM 270 CB ASN A 43 31.560 76.502 130.452 1.00 32.42 AATOM 271 CG ASN A 43 30.721 77.407 129.570 1.00 36.22 A ATOM 272 OD1 ASNA 43 31.175 78.472 129.145 1.00 39.75 A ATOM 273 ND2 ASN A 43 29.49276.985 129.285 1.00 38.09 A ATOM 274 C ASN A 43 33.494 74.939 130.6241.00 27.61 A ATOM 275 O ASN A 43 33.232 74.876 131.829 1.00 26.66 A ATOM276 N SER A 44 34.405 74.168 130.046 1.00 26.69 A ATOM 277 CA SER A 4435.125 73.152 130.799 1.00 27.90 A ATOM 278 CB SER A 44 34.892 71.781130.161 1.00 26.68 A ATOM 279 OG SER A 44 33.509 71.489 130.100 1.0028.08 A ATOM 280 C SER A 44 36.616 73.438 130.870 1.00 28.33 A ATOM 281O SER A 44 37.422 72.520 130.989 1.00 28.25 A ATOM 282 N GLU A 45 36.97374.717 130.803 1.00 30.31 A ATOM 283 CA GLU A 45 38.372 75.137 130.8551.00 32.52 A ATOM 284 CB GLU A 45 38.460 76.666 130.804 1.00 36.20 AATOM 285 CG GLU A 45 37.862 77.296 129.556 1.00 40.59 A ATOM 286 CD GLUA 45 38.635 76.954 128.297 1.00 43.46 A ATOM 287 OE1 GLU A 45 38.29077.492 127.224 1.00 44.77 A ATOM 288 OE2 GLU A 45 39.589 76.148 128.3781.00 46.65 A ATOM 289 C GLU A 45 39.082 74.635 132.109 1.00 31.09 A ATOM290 O GLU A 45 40.261 74.288 132.069 1.00 32.23 A ATOM 291 N HIS A 4638.356 74.590 133.220 1.00 30.26 A ATOM 292 CA HIS A 46 38.921 74.148134.489 1.00 30.21 A ATOM 293 CB HIS A 46 37.915 74.373 135.624 1.0030.18 A ATOM 294 CG HIS A 46 36.608 73.672 135.423 1.00 31.08 A ATOM 295CD2 HIS A 46 36.080 72.580 136.025 1.00 31.68 A ATOM 296 ND1 HIS A 4635.678 74.082 134.491 1.00 31.46 A ATOM 297 CE1 HIS A 46 34.635 73.272134.527 1.00 31.49 A ATOM 298 NE2 HIS A 46 34.854 72.352 135.450 1.0031.69 A ATOM 299 C HIS A 46 39.384 72.691 134.505 1.00 29.90 A ATOM 300O HIS A 46 40.153 72.301 135.383 1.00 28.22 A ATOM 301 N MET A 47 38.92071.891 133.544 1.00 29.28 A ATOM 302 CA MET A 47 39.307 70.477 133.4711.00 28.84 A ATOM 303 CB MET A 47 38.214 69.664 132.771 1.00 28.86 AATOM 304 CG MET A 47 36.808 69.935 133.286 1.00 30.82 A ATOM 305 SD META 47 35.578 68.879 132.493 1.00 31.81 A ATOM 306 CE MET A 47 35.68467.427 133.551 1.00 33.73 A ATOM 307 C MET A 47 40.621 70.327 132.7051.00 28.88 A ATOM 308 O MET A 47 40.689 69.627 131.693 1.00 27.03 A ATOM309 N THR A 48 41.665 70.983 133.199 1.00 29.25 A ATOM 310 CA THR A 4842.974 70.955 132.554 1.00 29.28 A ATOM 311 CB THR A 48 44.045 71.626133.450 1.00 30.40 A ATOM 312 OG1 THR A 48 44.133 70.932 134.699 1.0031.38 A ATOM 313 CG2 THR A 48 43.681 73.081 133.710 1.00 31.23 A ATOM314 C THR A 48 43.485 69.575 132.128 1.00 29.36 A ATOM 315 O THR A 4843.883 69.394 130.977 1.00 30.13 A ATOM 316 N ASP A 49 43.475 68.603133.036 1.00 28.72 A ATOM 317 CA ASP A 49 43.974 67.271 132.697 1.0029.59 A ATOM 318 CB ASP A 49 43.992 66.367 133.928 1.00 33.21 A ATOM 319CG ASP A 49 44.545 64.985 133.621 1.00 36.83 A ATOM 320 OD1 ASP A 4945.679 64.903 133.102 1.00 39.96 A ATOM 321 OD2 ASP A 49 43.850 63.981133.893 1.00 38.97 A ATOM 322 C ASP A 49 43.172 66.588 131.592 1.0028.05 A ATOM 323 O ASP A 49 43.744 66.023 130.660 1.00 28.22 A ATOM 324N LEU A 50 41.851 66.637 131.701 1.00 25.60 A ATOM 325 CA LEU A 5040.991 66.011 130.704 1.00 23.87 A ATOM 326 CB LEU A 50 39.527 66.120131.131 1.00 21.93 A ATOM 327 CG LEU A 50 38.534 65.261 130.350 1.0019.98 A ATOM 328 CD1 LEU A 50 38.945 63.789 130.429 1.00 19.09 A ATOM329 CD2 LEU A 50 37.146 65.460 130.927 1.00 20.31 A ATOM 330 C LEU A 5041.189 66.662 129.336 1.00 23.68 A ATOM 331 O LEU A 50 41.215 65.976128.313 1.00 22.19 A ATOM 332 N LYS A 51 41.332 67.985 129.316 1.0023.84 A ATOM 333 CA LYS A 51 41.532 68.686 128.052 1.00 25.09 A ATOM 334CB LYS A 51 41.650 70.199 128.283 1.00 25.49 A ATOM 335 CG LYS A 5141.828 71.005 126.999 1.00 26.33 A ATOM 336 CD LYS A 51 41.886 72.504127.280 1.00 28.75 A ATOM 337 CE LYS A 51 42.142 73.288 126.007 1.0029.76 A ATOM 338 NZ LYS A 51 42.144 74.756 126.260 1.00 30.99 A ATOM 339C LYS A 51 42.785 68.170 127.344 1.00 26.21 A ATOM 340 O LYS A 51 42.78267.971 126.130 1.00 24.74 A ATOM 341 N LYS A 52 43.856 67.949 128.1031.00 27.17 A ATOM 342 CA LYS A 52 45.098 67.449 127.516 1.00 28.10 AATOM 343 CB LYS A 52 46.194 67.352 128.582 1.00 30.83 A ATOM 344 CG LYSA 52 46.591 68.687 129.190 1.00 34.28 A ATOM 345 CD LYS A 52 47.63568.497 130.279 1.00 37.20 A ATOM 346 CE LYS A 52 47.985 69.816 130.9451.00 38.95 A ATOM 347 NZ LYS A 52 48.982 69.624 132.030 1.00 41.28 AATOM 348 C LYS A 52 44.873 66.076 126.888 1.00 26.97 A ATOM 349 O LYS A52 45.366 65.792 125.797 1.00 26.02 A ATOM 350 N LYS A 53 44.122 65.228127.583 1.00 26.21 A ATOM 351 CA LYS A 53 43.831 63.892 127.086 1.0025.04 A ATOM 352 CB LYS A 53 43.067 63.086 128.140 1.00 24.64 A ATOM 353CG LYS A 53 43.877 62.781 129.392 1.00 28.22 A ATOM 354 CD LYS A 5343.065 61.990 130.408 1.00 30.66 A ATOM 355 CE LYS A 53 43.880 61.718131.666 1.00 33.54 A ATOM 356 NZ LYS A 53 43.126 60.909 132.667 1.0036.02 A ATOM 357 C LYS A 53 43.012 63.962 125.798 1.00 23.42 A ATOM 358O LYS A 53 43.226 63.173 124.879 1.00 22.62 A ATOM 359 N PHE A 54 42.08664.915 125.732 1.00 23.36 A ATOM 360 CA PHE A 54 41.237 65.066 124.5501.00 22.90 A ATOM 361 CB PHE A 54 40.098 66.055 124.820 1.00 22.20 AATOM 362 CG PHE A 54 39.044 66.072 123.740 1.00 20.84 A ATOM 363 CD1 PHEA 54 38.409 64.897 123.352 1.00 19.63 A ATOM 364 CD2 PHE A 54 38.68267.260 123.115 1.00 20.10 A ATOM 365 CE1 PHE A 54 37.432 64.905 122.3571.00 18.43 A ATOM 366 CE2 PHE A 54 37.706 67.276 122.122 1.00 19.37 AATOM 367 CZ PHE A 54 37.081 66.097 121.742 1.00 18.82 A ATOM 368 C PHE A54 42.048 65.539 123.354 1.00 23.85 A ATOM 369 O PHE A 54 41.812 65.112122.219 1.00 23.78 A ATOM 370 N GLN A 55 43.000 66.432 123.603 1.0024.10 A ATOM 371 CA GLN A 55 43.842 66.930 122.528 1.00 24.91 A ATOM 372CB GLN A 55 44.832 67.974 123.062 1.00 26.37 A ATOM 373 CG GLN A 5545.921 68.373 122.072 1.00 28.68 A ATOM 374 CD GLN A 55 45.411 69.175120.884 1.00 30.30 A ATOM 375 OE1 GLN A 55 46.060 69.228 119.839 1.0031.71 A ATOM 376 NE2 GLN A 55 44.259 69.820 121.044 1.00 30.29 A ATOM377 C GLN A 55 44.586 65.725 121.967 1.00 24.46 A ATOM 378 O GLN A 5544.767 65.601 120.761 1.00 22.48 A ATOM 379 N ARG A 56 44.997 64.828122.858 1.00 24.95 A ATOM 380 CA ARG A 56 45.719 63.625 122.468 1.0025.91 A ATOM 381 CB ARG A 56 46.171 62.866 123.720 1.00 29.99 A ATOM 382CG ARG A 56 47.559 62.249 123.624 1.00 36.86 A ATOM 383 CD ARG A 5648.647 63.324 123.571 1.00 40.43 A ATOM 384 NE ARG A 56 48.699 64.137124.787 1.00 44.69 A ATOM 385 CZ ARG A 56 48.992 63.667 125.998 1.0046.01 A ATOM 386 NH1 ARG A 56 49.263 62.379 126.168 1.00 47.48 A ATOM387 NH2 ARG A 56 49.015 64.485 127.044 1.00 46.66 A ATOM 388 C ARG A 5644.804 62.739 121.618 1.00 24.27 A ATOM 389 O ARG A 56 45.215 62.221120.574 1.00 24.04 A ATOM 390 N ILE A 57 43.565 62.572 122.075 1.0021.82 A ATOM 391 CA ILE A 57 42.579 61.765 121.367 1.00 20.34 A ATOM 392CB ILE A 57 41.237 61.729 122.129 1.00 20.57 A ATOM 393 CG2 ILE A 5740.154 61.093 121.261 1.00 21.54 A ATOM 394 CG1 ILE A 57 41.399 60.948123.438 1.00 20.21 A ATOM 395 CD1 ILE A 57 40.171 60.973 124.315 1.0019.50 A ATOM 396 C ILE A 57 42.337 62.329 119.968 1.00 20.51 A ATOM 397O ILE A 57 42.396 61.599 118.986 1.00 20.89 A ATOM 398 N CYS A 58 42.07663.630 119.879 1.00 19.30 A ATOM 399 CA CYS A 58 41.823 64.251 118.5871.00 20.99 A ATOM 400 CB CYS A 58 41.533 65.745 118.759 1.00 19.32 AATOM 401 SG CYS A 58 39.917 66.082 119.509 1.00 18.88 A ATOM 402 C CYS A58 42.966 64.047 117.601 1.00 22.44 A ATOM 403 O CYS A 58 42.732 63.850116.412 1.00 23.07 A ATOM 404 N GLU A 59 44.200 64.077 118.092 1.0024.02 A ATOM 405 CA GLU A 59 45.363 63.892 117.225 1.00 26.24 A ATOM 406CB GLU A 59 46.644 64.284 117.972 1.00 28.50 A ATOM 407 CG GLU A 5946.606 65.706 118.527 1.00 33.23 A ATOM 408 CD GLU A 59 47.855 66.085119.315 1.00 35.09 A ATOM 409 OE1 GLU A 59 48.343 65.248 120.109 1.0036.66 A ATOM 410 OE2 GLU A 59 48.338 67.227 119.149 1.00 34.23 A ATOM411 C GLU A 59 45.455 62.445 116.741 1.00 26.77 A ATOM 412 O GLU A 5945.872 62.177 115.614 1.00 26.70 A ATOM 413 N ARG A 60 45.046 61.518117.596 1.00 26.73 A ATOM 414 CA ARG A 60 45.079 60.100 117.264 1.0028.79 A ATOM 415 CB ARG A 60 44.919 59.274 118.544 1.00 33.01 A ATOM 416CG ARG A 60 46.132 59.301 119.456 1.00 39.19 A ATOM 417 CD ARG A 6047.211 58.346 118.956 1.00 45.62 A ATOM 418 NE ARG A 60 47.412 57.224119.875 1.00 49.49 A ATOM 419 CZ ARG A 60 46.455 56.383 120.261 1.0051.76 A ATOM 420 NH1 ARG A 60 45.215 56.526 119.809 1.00 52.07 A ATOM421 NH2 ARG A 60 46.735 55.399 121.109 1.00 53.18 A ATOM 422 C ARG A 6044.024 59.664 116.240 1.00 25.81 A ATOM 423 O ARG A 60 44.225 58.686115.524 1.00 23.81 A ATOM 424 N THR A 61 42.911 60.388 116.160 1.0023.41 A ATOM 425 CA THR A 61 41.834 60.023 115.235 1.00 22.16 A ATOM 426CB THR A 61 40.629 60.966 115.359 1.00 19.80 A ATOM 427 OG1 THR A 6141.003 62.269 114.896 1.00 17.03 A ATOM 428 CG2 THR A 61 40.150 61.047116.802 1.00 20.05 A ATOM 429 C THR A 61 42.237 60.045 113.768 1.0022.06 A ATOM 430 O THR A 61 41.616 59.382 112.942 1.00 20.90 A ATOM 431N GLN A 62 43.275 60.814 113.457 1.00 21.51 A ATOM 432 CA GLN A 6243.749 60.979 112.089 1.00 21.94 A ATOM 433 CB GLN A 62 44.232 59.649111.503 1.00 24.19 A ATOM 434 CG GLN A 62 45.428 59.093 112.270 1.0025.12 A ATOM 435 CD GLN A 62 46.325 58.218 111.429 1.00 28.57 A ATOM 436OE1 GLN A 62 45.857 57.352 110.687 1.00 28.23 A ATOM 437 NE2 GLN A 6247.633 58.430 111.550 1.00 29.81 A ATOM 438 C GLN A 62 42.654 61.602111.227 1.00 21.62 A ATOM 439 O GLN A 62 42.545 61.345 110.021 1.0021.13 A ATOM 440 N ILE A 63 41.829 62.413 111.881 1.00 18.54 A ATOM 441CA ILE A 63 40.763 63.155 111.220 1.00 16.85 A ATOM 442 CB ILE A 6339.475 63.188 112.062 1.00 15.18 A ATOM 443 CG2 ILE A 63 38.482 64.153111.446 1.00 17.26 A ATOM 444 CG1 ILE A 63 38.854 61.793 112.138 1.0013.24 A ATOM 445 CD1 ILE A 63 37.704 61.705 113.129 1.00 12.22 A ATOM446 C ILE A 63 41.334 64.572 111.167 1.00 18.36 A ATOM 447 O ILE A 6341.882 65.053 112.160 1.00 17.80 A ATOM 448 N LYS A 64 41.227 65.231110.022 1.00 18.39 A ATOM 449 CA LYS A 64 41.757 66.587 109.884 1.0020.17 A ATOM 450 CB LYS A 64 42.534 66.715 108.568 1.00 21.80 A ATOM 451CG LYS A 64 43.868 65.976 108.573 1.00 27.09 A ATOM 452 CD LYS A 6444.813 66.599 109.588 1.00 31.09 A ATOM 453 CE LYS A 64 46.056 65.749109.806 1.00 33.75 A ATOM 454 NZ LYS A 64 45.731 64.450 110.462 1.0036.45 A ATOM 455 C LYS A 64 40.661 67.637 109.930 1.00 20.31 A ATOM 456O LYS A 64 40.845 68.725 110.491 1.00 17.10 A ATOM 457 N ASN A 65 39.52067.301 109.335 1.00 19.52 A ATOM 458 CA ASN A 65 38.376 68.206 109.2731.00 19.30 A ATOM 459 CB ASN A 65 38.409 68.985 107.950 1.00 21.83 AATOM 460 CG ASN A 65 37.084 69.676 107.634 1.00 25.41 A ATOM 461 OD1 ASNA 65 36.120 69.041 107.184 1.00 26.40 A ATOM 462 ND2 ASN A 65 37.03170.978 107.871 1.00 24.80 A ATOM 463 C ASN A 65 37.056 67.454 109.3911.00 18.97 A ATOM 464 O ASN A 65 36.943 66.299 108.969 1.00 17.44 A ATOM465 N ARG A 66 36.069 68.117 109.986 1.00 18.13 A ATOM 466 CA ARG A 6634.733 67.553 110.146 1.00 16.96 A ATOM 467 CB ARG A 66 34.529 67.023111.566 1.00 16.26 A ATOM 468 CG ARG A 66 35.173 65.679 111.852 1.0016.61 A ATOM 469 CD ARG A 66 34.738 65.183 113.224 1.00 16.24 A ATOM 470NE ARG A 66 35.405 65.920 114.289 1.00 15.56 A ATOM 471 CZ ARG A 6634.992 65.947 115.550 1.00 17.32 A ATOM 472 NH1 ARG A 66 33.901 65.287115.908 1.00 17.58 A ATOM 473 NH2 ARG A 66 35.685 66.616 116.465 1.0017.79 A ATOM 474 C ARG A 66 33.701 68.637 109.880 1.00 17.04 A ATOM 475O ARG A 66 33.912 69.796 110.237 1.00 17.53 A ATOM 476 N HIS A 67 32.60268.277 109.228 1.00 15.73 A ATOM 477 CA HIS A 67 31.546 69.245 108.9841.00 17.68 A ATOM 478 CB HIS A 67 30.864 68.997 107.635 1.00 18.72 AATOM 479 CG HIS A 67 31.713 69.348 106.454 1.00 21.98 A ATOM 480 CD2 HISA 67 31.716 70.441 105.653 1.00 20.76 A ATOM 481 ND1 HIS A 67 32.71468.527 105.982 1.00 21.72 A ATOM 482 CE1 HIS A 67 33.295 69.097 104.9411.00 21.39 A ATOM 483 NE2 HIS A 67 32.707 70.259 104.721 1.00 23.60 AATOM 484 C HIS A 67 30.540 69.069 110.118 1.00 18.33 A ATOM 485 O HIS A67 30.176 67.941 110.464 1.00 17.18 A ATOM 486 N MET A 68 30.117 70.178110.713 1.00 16.86 A ATOM 487 CA MET A 68 29.163 70.124 111.807 1.0020.49 A ATOM 488 CB MET A 68 29.893 70.228 113.155 1.00 23.32 A ATOM 489CG MET A 68 30.914 69.116 113.386 1.00 28.72 A ATOM 490 SD MET A 6831.545 69.023 115.086 1.00 37.96 A ATOM 491 CE MET A 68 31.064 67.331115.520 1.00 34.14 A ATOM 492 C MET A 68 28.106 71.213 111.710 1.0019.55 A ATOM 493 O MET A 68 28.424 72.397 111.603 1.00 19.23 A ATOM 494N TYR A 69 26.844 70.800 111.736 1.00 19.71 A ATOM 495 CA TYR A 6925.733 71.738 111.685 1.00 20.15 A ATOM 496 CB TYR A 69 24.401 70.981111.659 1.00 20.47 A ATOM 497 CG TYR A 69 23.253 71.748 112.277 1.0020.28 A ATOM 498 CD1 TYR A 69 22.713 72.874 111.650 1.00 22.00 A ATOM499 CE1 TYR A 69 21.668 73.595 112.239 1.00 22.79 A ATOM 500 CD2 TYR A69 22.723 71.363 113.502 1.00 20.81 A ATOM 501 CE2 TYR A 69 21.68872.069 114.094 1.00 21.13 A ATOM 502 CZ TYR A 69 21.163 73.184 113.4611.00 22.53 A ATOM 503 OH TYR A 69 20.136 73.877 114.063 1.00 22.91 AATOM 504 C TYR A 69 25.789 72.632 112.918 1.00 19.58 A ATOM 505 O TYR A69 25.474 73.820 112.853 1.00 18.63 A ATOM 506 N LEU A 70 26.195 72.052114.044 1.00 17.07 A ATOM 507 CA LEU A 70 26.286 72.799 115.290 1.0018.70 A ATOM 508 CB LEU A 70 26.548 71.846 116.466 1.00 16.86 A ATOM 509CG LEU A 70 25.399 70.921 116.867 1.00 17.66 A ATOM 510 CD1 LEU A 7025.866 69.928 117.930 1.00 17.33 A ATOM 511 CD2 LEU A 70 24.229 71.755117.384 1.00 16.30 A ATOM 512 C LEU A 70 27.387 73.842 115.230 1.0019.34 A ATOM 513 O LEU A 70 28.546 73.515 114.963 1.00 19.14 A ATOM 514N THR A 71 27.017 75.094 115.483 1.00 19.06 A ATOM 515 CA THR A 7127.965 76.198 115.478 1.00 19.11 A ATOM 516 CB THR A 71 27.529 77.305114.514 1.00 20.64 A ATOM 517 OG1 THR A 71 26.319 77.892 114.997 1.0018.72 A ATOM 518 CG2 THR A 71 27.288 76.737 113.123 1.00 21.99 A ATOM519 C THR A 71 28.023 76.794 116.878 1.00 19.23 A ATOM 520 O THR A 7127.180 76.500 117.727 1.00 17.80 A ATOM 521 N GLU A 72 29.015 77.644117.118 1.00 19.93 A ATOM 522 CA GLU A 72 29.164 78.269 118.425 1.0021.10 A ATOM 523 CB GLU A 72 30.386 79.196 118.431 1.00 22.65 A ATOM 524CG GLU A 72 30.715 79.745 119.814 1.00 25.51 A ATOM 525 CD GLU A 7232.066 80.436 119.887 1.00 26.76 A ATOM 526 OE1 GLU A 72 32.356 81.053120.939 1.00 29.43 A ATOM 527 OE2 GLU A 72 32.835 80.361 118.908 1.0025.78 A ATOM 528 C GLU A 72 27.908 79.049 118.806 1.00 21.16 A ATOM 529O GLU A 72 27.479 79.035 119.965 1.00 19.47 A ATOM 530 N GLU A 73 27.31579.727 117.830 1.00 22.57 A ATOM 531 CA GLU A 73 26.108 80.506 118.0821.00 23.75 A ATOM 532 CB GLU A 73 25.756 81.340 116.849 1.00 28.49 AATOM 533 CG GLU A 73 26.548 82.651 116.717 1.00 35.51 A ATOM 534 CD GLUA 73 27.929 82.617 117.382 1.00 41.12 A ATOM 535 OE1 GLU A 73 27.99582.619 118.635 1.00 43.42 A ATOM 536 OE2 GLU A 73 28.950 82.594 116.6561.00 44.19 A ATOM 537 C GLU A 73 24.947 79.594 118.466 1.00 21.96 A ATOM538 O GLU A 73 24.190 79.895 119.390 1.00 20.37 A ATOM 539 N ILE A 7424.810 78.470 117.770 1.00 19.89 A ATOM 540 CA ILE A 74 23.738 77.535118.089 1.00 18.76 A ATOM 541 CB ILE A 74 23.659 76.390 117.043 1.0018.90 A ATOM 542 CG2 ILE A 74 22.714 75.295 117.521 1.00 16.71 A ATOM543 CG1 ILE A 74 23.170 76.954 115.705 1.00 20.30 A ATOM 544 CD1 ILE A74 23.046 75.924 114.596 1.00 18.88 A ATOM 545 C ILE A 74 23.964 76.960119.493 1.00 18.52 A ATOM 546 O ILE A 74 23.041 76.895 120.306 1.0020.62 A ATOM 547 N LEU A 75 25.193 76.561 119.788 1.00 18.16 A ATOM 548CA LEU A 75 25.498 76.010 121.104 1.00 17.27 A ATOM 549 CB LEU A 7526.954 75.553 121.153 1.00 17.79 A ATOM 550 CG LEU A 75 27.280 74.382120.222 1.00 14.50 A ATOM 551 CD1 LEU A 75 28.761 74.033 120.299 1.0015.68 A ATOM 552 CD2 LEU A 75 26.416 73.189 120.613 1.00 18.83 A ATOM553 C LEU A 75 25.225 77.028 122.212 1.00 19.75 A ATOM 554 O LEU A 7524.815 76.666 123.318 1.00 18.99 A ATOM 555 N LYS A 76 25.441 78.303121.906 1.00 20.65 A ATOM 556 CA LYS A 76 25.212 79.369 122.874 1.0023.67 A ATOM 557 CB LYS A 76 25.660 80.713 122.294 1.00 25.80 A ATOM 558CG LYS A 76 25.558 81.874 123.277 1.00 31.54 A ATOM 559 CD LYS A 7625.830 83.205 122.590 1.00 34.91 A ATOM 560 CE LYS A 76 25.581 84.377123.528 1.00 36.18 A ATOM 561 NZ LYS A 76 25.622 85.681 122.801 1.0039.35 A ATOM 562 C LYS A 76 23.734 79.434 123.251 1.00 23.97 A ATOM 563O LYS A 76 23.389 79.720 124.395 1.00 23.57 A ATOM 564 N GLU A 77 22.86579.152 122.283 1.00 23.60 A ATOM 565 CA GLU A 77 21.424 79.182 122.5161.00 25.27 A ATOM 566 CB GLU A 77 20.668 79.378 121.197 1.00 27.47 AATOM 567 CG GLU A 77 21.266 80.405 120.247 1.00 34.00 A ATOM 568 CD GLUA 77 21.546 81.740 120.909 1.00 36.99 A ATOM 569 OE1 GLU A 77 20.63382.284 121.566 1.00 40.32 A ATOM 570 OE2 GLU A 77 22.679 82.250 120.7641.00 40.16 A ATOM 571 C GLU A 77 20.941 77.886 123.161 1.00 24.62 A ATOM572 O GLU A 77 19.773 77.770 123.521 1.00 24.54 A ATOM 573 N ASN A 7821.838 76.913 123.307 1.00 22.72 A ATOM 574 CA ASN A 78 21.468 75.627123.884 1.00 22.16 A ATOM 575 CB ASN A 78 21.406 74.571 122.782 1.0020.72 A ATOM 576 CG ASN A 78 20.246 74.789 121.843 1.00 21.61 A ATOM 577OD1 ASN A 78 19.115 74.375 122.123 1.00 19.12 A ATOM 578 ND2 ASN A 7820.512 75.457 120.724 1.00 18.54 A ATOM 579 C ASN A 78 22.402 75.146124.984 1.00 22.23 A ATOM 580 O ASN A 78 23.104 74.149 124.820 1.0022.58 A ATOM 581 N PRO A 79 22.412 75.844 126.130 1.00 21.67 A ATOM 582CD PRO A 79 21.562 76.985 126.514 1.00 21.10 A ATOM 583 CA PRO A 7923.283 75.441 127.237 1.00 21.96 A ATOM 584 CB PRO A 79 22.958 76.465128.327 1.00 22.78 A ATOM 585 CG PRO A 79 21.530 76.853 128.023 1.0023.42 A ATOM 586 C PRO A 79 23.036 74.000 127.689 1.00 22.12 A ATOM 587O PRO A 79 23.959 73.316 128.119 1.00 20.55 A ATOM 588 N ASN A 80 21.79373.537 127.594 1.00 21.11 A ATOM 589 CA ASN A 80 21.489 72.173 128.0061.00 22.35 A ATOM 590 CB ASN A 80 19.982 71.931 128.012 1.00 24.80 AATOM 591 CG ASN A 80 19.266 72.794 129.026 1.00 27.03 A ATOM 592 OD1 ASNA 80 19.790 73.058 130.109 1.00 27.86 A ATOM 593 ND2 ASN A 80 18.06073.233 128.687 1.00 30.50 A ATOM 594 C ASN A 80 22.184 71.144 127.1181.00 22.01 A ATOM 595 O ASN A 80 22.410 70.009 127.536 1.00 21.27 A ATOM596 N MET A 81 22.530 71.541 125.898 1.00 20.53 A ATOM 597 CA MET A 8123.221 70.635 124.986 1.00 21.23 A ATOM 598 CB MET A 81 22.919 70.996123.523 1.00 20.11 A ATOM 599 CG MET A 81 21.541 70.549 123.044 1.0017.66 A ATOM 600 SD MET A 81 21.145 71.070 121.348 1.00 20.66 A ATOM 601CE MET A 81 22.478 70.287 120.420 1.00 19.72 A ATOM 602 C MET A 8124.728 70.677 125.235 1.00 20.83 A ATOM 603 O MET A 81 25.447 69.745124.884 1.00 19.87 A ATOM 604 N CYS A 82 25.203 71.758 125.850 1.0020.43 A ATOM 605 CA CYS A 82 26.625 71.890 126.140 1.00 20.36 A ATOM 606CB CYS A 82 27.016 73.365 126.252 1.00 19.40 A ATOM 607 SG CYS A 8226.921 74.261 124.692 1.00 22.96 A ATOM 608 C CYS A 82 26.971 71.159127.428 1.00 19.46 A ATOM 609 O CYS A 82 28.126 70.807 127.664 1.0021.85 A ATOM 610 N ALA A 83 25.963 70.932 128.261 1.00 19.79 A ATOM 611CA ALA A 83 26.167 70.232 129.518 1.00 19.82 A ATOM 612 CB ALA A 8324.960 70.417 130.414 1.00 20.37 A ATOM 613 C ALA A 83 26.361 68.756129.207 1.00 21.03 A ATOM 614 O ALA A 83 25.891 68.272 128.175 1.0018.48 A ATOM 615 N TYR A 84 27.053 68.043 130.091 1.00 20.86 A ATOM 616CA TYR A 84 27.269 66.615 129.883 1.00 21.75 A ATOM 617 CB TYR A 8428.207 66.045 130.946 1.00 20.13 A ATOM 618 CG TYR A 84 28.198 64.531130.988 1.00 20.20 A ATOM 619 CD1 TYR A 84 28.805 63.782 129.986 1.0019.11 A ATOM 620 CE1 TYR A 84 28.762 62.387 130.008 1.00 21.15 A ATOM621 CD2 TYR A 84 27.547 63.850 132.017 1.00 19.79 A ATOM 622 CE2 TYR A84 27.495 62.468 132.047 1.00 23.38 A ATOM 623 CZ TYR A 84 28.101 61.740131.044 1.00 21.82 A ATOM 624 OH TYR A 84 28.027 60.369 131.072 1.0022.42 A ATOM 625 C TYR A 84 25.936 65.885 129.969 1.00 22.94 A ATOM 626O TYR A 84 25.678 64.949 129.212 1.00 24.58 A ATOM 627 N LYS A 85 25.09166.329 130.895 1.00 24.59 A ATOM 628 CA LYS A 85 23.786 65.715 131.1161.00 27.30 A ATOM 629 CB LYS A 85 23.937 64.572 132.128 1.00 28.97 AATOM 630 CG LYS A 85 22.680 64.203 132.905 1.00 33.37 A ATOM 631 CD LYSA 85 23.016 63.202 134.011 1.00 35.36 A ATOM 632 CE LYS A 85 21.85663.001 134.975 1.00 36.29 A ATOM 633 NZ LYS A 85 20.630 62.504 134.2891.00 37.50 A ATOM 634 C LYS A 85 22.743 66.717 131.613 1.00 26.53 A ATOM635 O LYS A 85 22.744 67.089 132.786 1.00 28.76 A ATOM 636 N ALA A 8621.862 67.150 130.713 1.00 23.82 A ATOM 637 CA ALA A 86 20.789 68.089131.040 1.00 21.57 A ATOM 638 CB ALA A 86 21.283 69.519 130.892 1.0020.90 A ATOM 639 C ALA A 86 19.638 67.823 130.065 1.00 21.98 A ATOM 640O ALA A 86 19.885 67.469 128.913 1.00 20.68 A ATOM 641 N PRO A 87 18.37467.982 130.513 1.00 23.00 A ATOM 642 CD PRO A 87 17.985 68.429 131.8641.00 25.15 A ATOM 643 CA PRO A 87 17.179 67.756 129.682 1.00 23.11 AATOM 644 CB PRO A 87 16.046 68.277 130.561 1.00 25.66 A ATOM 645 CG PROA 87 16.553 67.972 131.951 1.00 26.07 A ATOM 646 C PRO A 87 17.29068.510 128.368 1.00 23.09 A ATOM 647 O PRO A 87 17.312 69.741 128.3631.00 20.97 A ATOM 648 N SER A 88 17.342 67.780 127.253 1.00 19.74 A ATOM649 CA SER A 88 17.517 68.434 125.962 1.00 16.92 A ATOM 650 CB SER A 8818.992 68.805 125.804 1.00 16.86 A ATOM 651 OG SER A 88 19.797 67.642125.909 1.00 14.70 A ATOM 652 C SER A 88 17.095 67.626 124.737 1.0017.40 A ATOM 653 O SER A 88 17.387 68.027 123.613 1.00 17.18 A ATOM 654N LEU A 89 16.419 66.499 124.931 1.00 16.77 A ATOM 655 CA LEU A 8916.011 65.691 123.786 1.00 18.16 A ATOM 656 CB LEU A 89 15.315 64.408124.245 1.00 19.74 A ATOM 657 CG LEU A 89 14.896 63.525 123.066 1.0020.68 A ATOM 658 CD1 LEU A 89 16.117 62.910 122.420 1.00 20.92 A ATOM659 CD2 LEU A 89 13.971 62.457 123.551 1.00 22.54 A ATOM 660 C LEU A 8915.107 66.441 122.808 1.00 17.08 A ATOM 661 O LEU A 89 15.295 66.344121.598 1.00 18.35 A ATOM 662 N ASP A 90 14.135 67.191 123.320 1.0017.39 A ATOM 663 CA ASP A 90 13.222 67.943 122.453 1.00 16.14 A ATOM 664CB ASP A 90 12.218 68.737 123.294 1.00 19.36 A ATOM 665 CG ASP A 9011.162 67.858 123.942 1.00 20.42 A ATOM 666 OD1 ASP A 90 10.253 68.421124.581 1.00 22.07 A ATOM 667 OD2 ASP A 90 11.234 66.612 123.821 1.0021.79 A ATOM 668 C ASP A 90 13.959 68.906 121.511 1.00 17.32 A ATOM 669O ASP A 90 13.725 68.920 120.291 1.00 14.74 A ATOM 670 N ALA A 91 14.83369.729 122.078 1.00 15.85 A ATOM 671 CA ALA A 91 15.593 70.679 121.2731.00 16.35 A ATOM 672 CB ALA A 91 16.476 71.533 122.175 1.00 16.94 AATOM 673 C ALA A 91 16.449 69.951 120.235 1.00 16.25 A ATOM 674 O ALA A91 16.524 70.369 119.076 1.00 13.95 A ATOM 675 N ARG A 92 17.085 68.855120.647 1.00 14.79 A ATOM 676 CA ARG A 92 17.937 68.091 119.739 1.0014.64 A ATOM 677 CB ARG A 92 18.672 66.981 120.499 1.00 14.18 A ATOM 678CG ARG A 92 19.654 67.461 121.572 1.00 13.74 A ATOM 679 CD ARG A 92.20.045 66.282 122.463 1.00 13.80 A ATOM 680 NE ARG A 92 20.992 66.630123.523 1.00 13.20 A ATOM 681 CZ ARG A 92 22.310 66.719 123.359 1.0013.36 A ATOM 682 NH1 ARG A 92 22.858 66.491 122.171 1.00 12.28 A ATOM683 NH2 ARG A 92 23.087 67.010 124.398 1.00 15.07 A ATOM 684 C ARG A 9217.130 67.475 118.598 1.00 14.35 A ATOM 685 O ARG A 92 17.492 67.605117.432 1.00 13.62 A ATOM 686 N GLU A 93 16.037 66.803 118.939 1.0014.60 A ATOM 687 CA GLU A 93 15.192 66.178 117.925 1.00 15.88 A ATOM 688CB GLU A 93 14.073 65.379 118.597 1.00 16.99 A ATOM 689 CG GLU A 9314.580 64.128 119.313 1.00 20.99 A ATOM 690 CD GLU A 93 15.046 63.032118.348 1.00 23.76 A ATOM 691 OE1 GLU A 93 16.010 62.305 118.675 1.0023.78 A ATOM 692 OE2 GLU A 93 14.442 62.889 117.267 1.00 26.26 A ATOM693 C GLU A 93 14.614 67.214 116.966 1.00 15.22 A ATOM 694 O GLU A 9314.458 66.947 115.776 1.00 15.96 A ATOM 695 N ASP A 94 14.309 68.406117.465 1.00 15.22 A ATOM 696 CA ASP A 94 13.777 69.430 116.576 1.0014.70 A ATOM 697 CB ASP A 94 13.340 70.673 117.360 1.00 17.50 A ATOM 698CG ASP A 94 12.052 70.448 118.151 1.00 21.10 A ATOM 699 OD1 ASP A 9411.253 69.564 117.768 1.00 23.41 A ATOM 700 OD2 ASP A 94 11.826 71.167119.150 1.00 23.08 A ATOM 701 C ASP A 94 14.829 69.801 115.530 1.0015.14 A ATOM 702 O ASP A 94 14.501 70.018 114.364 1.00 14.99 A ATOM 703N MET A 95 16.094 69.860 115.944 1.00 16.52 A ATOM 704 CA MET A 9517.183 70.187 115.031 1.00 13.82 A ATOM 705 CB MET A 95 18.507 70.321115.789 1.00 14.37 A ATOM 706 CG MET A 95 18.598 71.520 116.725 1.0015.94 A ATOM 707 SD MET A 95 20.178 71.517 117.624 1.00 19.13 A ATOM 708CE MET A 95 20.074 73.098 118.500 1.00 19.01 A ATOM 709 C MET A 9517.316 69.071 114.003 1.00 15.95 A ATOM 710 O MET A 95 17.440 69.324112.806 1.00 15.19 A ATOM 711 N MET A 96 17.313 67.833 114.490 1.0014.58 A ATOM 712 CA MET A 96 17.428 66.670 113.618 1.00 14.52 A ATOM 713CB MET A 96 17.341 65.376 114.447 1.00 13.66 A ATOM 714 CG MET A 9618.498 65.155 115.417 1.00 15.74 A ATOM 715 SD MET A 96 20.095 64.978114.615 1.00 18.80 A ATOM 716 CE MET A 96 20.010 63.239 114.121 1.0015.04 A ATOM 717 C MET A 96 16.328 66.673 112.554 1.00 14.12 A ATOM 718O MET A 96 16.609 66.556 111.366 1.00 17.99 A ATOM 719 N ILE A 97 15.07966.806 112.983 1.00 14.93 A ATOM 720 CA ILE A 97 13.944 66.804 112.0581.00 15.15 A ATOM 721 CB ILE A 97 12.615 66.959 112.835 1.00 15.85 AATOM 722 CG2 ILE A 97 11.431 67.096 111.861 1.00 17.38 A ATOM 723 CG1ILE A 97 12.405 65.737 113.735 1.00 13.08 A ATOM 724 CD1 ILE A 97 11.27765.901 114.736 1.00 14.10 A ATOM 725 C ILE A 97 14.062 67.891 110.9841.00 16.23 A ATOM 726 O ILE A 97 13.664 67.694 109.829 1.00 15.33 A ATOM727 N ARG A 98 14.624 69.033 111.356 1.00 15.97 A ATOM 728 CA ARG A 9814.796 70.123 110.400 1.00 18.43 A ATOM 729 CB ARG A 98 15.015 71.435111.150 1.00 19.15 A ATOM 730 CG ARG A 98 15.092 72.667 110.267 1.0024.01 A ATOM 731 CD ARG A 98 15.425 73.900 111.093 1.00 25.52 A ATOM 732NE ARG A 98 14.794 73.866 112.412 1.00 27.90 A ATOM 733 CZ ARG A 9815.447 73.645 113.548 1.00 27.71 A ATOM 734 NH1 ARG A 98 16.758 73.437113.529 1.00 33.63 A ATOM 735 NH2 ARG A 98 14.793 73.635 114.704 1.0031.02 A ATOM 736 C ARG A 98 15.979 69.889 109.456 1.00 17.85 A ATOM 737O ARG A 98 15.850 69.980 108.230 1.00 16.62 A ATOM 738 N GLU A 99 17.12769.561 110.034 1.00 16.61 A ATOM 739 CA GLU A 99 18.352 69.379 109.2671.00 16.47 A ATOM 740 CB GLU A 99 19.543 69.659 110.181 1.00 17.68 AATOM 741 CG GLU A 99 19.471 71.041 110.816 1.00 19.11 A ATOM 742 CD GLUA 99 19.564 72.152 109.786 1.00 21.20 A ATOM 743 OE1 GLU A 99 19.07473.271 110.061 1.00 23.07 A ATOM 744 OE2 GLU A 99 20.139 71.904 108.7051.00 21.85 A ATOM 745 C GLU A 99 18.598 68.083 108.514 1.00 16.27 A ATOM746 O GLU A 99 19.213 68.098 107.449 1.00 16.09 A ATOM 747 N VAL A 10018.141 66.962 109.053 1.00 15.95 A ATOM 748 CA VAL A 100 18.379 65.681108.402 1.00 16.57 A ATOM 749 CB VAL A 100 17.809 64.528 109.258 1.0018.24 A ATOM 750 CG1 VAL A 100 17.921 63.197 108.521 1.00 20.43 A ATOM751 CG2 VAL A 100 18.591 64.453 110.562 1.00 19.88 A ATOM 752 C VAL A100 17.827 65.644 106.980 1.00 16.27 A ATOM 753 O VAL A 100 18.54865.308 106.041 1.00 14.58 A ATOM 754 N PRO A 101 16.549 66.013 106.7921.00 18.57 A ATOM 755 CD PRO A 101 15.480 66.240 107.782 1.00 20.19 AATOM 756 CA PRO A 101 16.013 65.983 105.425 1.00 18.96 A ATOM 757 CB PROA 101 14.503 66.063 105.646 1.00 20.79 A ATOM 758 CG PRO A 101 14.37966.821 106.941 1.00 21.86 A ATOM 759 C PRO A 101 16.540 67.100 104.5221.00 17.94 A ATOM 760 O PRO A 101 16.618 66.945 103.308 1.00 18.12 AATOM 761 N ARG A 102 16.910 68.222 105.122 1.00 18.08 A ATOM 762 CA ARGA 102 17.411 69.361 104.365 1.00 19.16 A ATOM 763 CB ARG A 102 17.53070.555 105.314 1.00 22.01 A ATOM 764 CG ARG A 102 18.080 71.815 104.7121.00 26.94 A ATOM 765 CD ARG A 102 17.796 72.989 105.634 1.00 28.29 AATOM 766 NE ARG A 102 18.545 74.166 105.225 1.00 30.92 A ATOM 767 CZ ARGA 102 19.826 74.361 105.506 1.00 32.08 A ATOM 768 NH1 ARG A 102 20.49673.459 106.210 1.00 31.02 A ATOM 769 NH2 ARG A 102 20.441 75.449 105.0591.00 33.44 A ATOM 770 C ARG A 102 18.741 69.055 103.664 1.00 18.26 AATOM 771 O ARG A 102 18.887 69.286 102.464 1.00 18.02 A ATOM 772 N VAL A103 19.705 68.517 104.402 1.00 15.63 A ATOM 773 CA VAL A 103 20.99968.175 103.817 1.00 16.43 A ATOM 774 CB VAL A 103 22.037 67.828 104.9071.00 16.44 A ATOM 775 CG1 VAL A 103 23.378 67.471 104.263 1.00 17.24 AATOM 776 CG2 VAL A 103 22.194 69.011 105.856 1.00 19.29 A ATOM 777 C VALA 103 20.795 66.967 102.911 1.00 15.93 A ATOM 778 O VAL A 103 21.45266.834 101.881 1.00 14.17 A ATOM 779 N GLY A 104 19.871 66.094 103.3021.00 16.69 A ATOM 780 CA GLY A 104 19.580 64.918 102.499 1.00 14.99 AATOM 781 C GLY A 104 19.068 65.333 101.126 1.00 16.35 A ATOM 782 O GLY A104 19.437 64.745 100.112 1.00 17.10 A ATOM 783 N LYS A 105 18.22166.356 101.084 1.00 16.15 A ATOM 784 CA LYS A 105 17.702 66.820 99.8031.00 17.34 A ATOM 785 CB LYS A 105 16.675 67.936 99.990 1.00 17.80 AATOM 786 CG LYS A 105 16.189 68.486 98.653 1.00 21.22 A ATOM 787 CD LYSA 105 15.789 69.941 98.756 1.00 25.56 A ATOM 788 CE LYS A 105 15.60070.553 97.374 1.00 28.16 A ATOM 789 NZ LYS A 105 16.888 70.618 96.6201.00 29.98 A ATOM 790 C LYS A 105 18.818 67.336 98.902 1.00 16.20 A ATOM791 O LYS A 105 18.807 67.091 97.700 1.00 17.34 A ATOM 792 N GLU A 10619.773 68.062 99.477 1.00 16.91 A ATOM 793 CA GLU A 106 20.881 68.59898.696 1.00 19.15 A ATOM 794 CB GLU A 106 21.835 69.387 99.600 1.0020.83 A ATOM 795 CG GLU A 106 23.047 69.922 98.862 1.00 25.52 A ATOM 796CD GLU A 106 23.920 70.828 99.716 1.00 26.98 A ATOM 797 OE1 GLU A 10625.035 71.164 99.260 1.00 27.30 A ATOM 798 OE2 GLU A 106 23.495 71.204100.832 1.00 27.96 A ATOM 799 C GLU A 106 21.629 67.450 98.016 1.0018.67 A ATOM 800 O GLU A 106 21.938 67.504 96.817 1.00 16.99 A ATOM 801N ALA A 107 21.907 66.401 98.783 1.00 15.83 A ATOM 802 CA ALA A 10722.610 65.244 98.243 1.00 15.27 A ATOM 803 CB ALA A 107 22.928 64.25199.359 1.00 14.32 A ATOM 804 C ALA A 107 21.778 64.556 97.162 1.00 13.90A ATOM 805 O ALA A 107 22.299 64.189 96.105 1.00 13.71 A ATOM 806 N ALAA 108 20.488 64.380 97.431 1.00 14.03 A ATOM 807 CA ALA A 108 19.59963.720 96.477 1.00 15.72 A ATOM 808 CB ALA A 108 18.219 63.519 97.0911.00 15.61 A ATOM 809 C ALA A 108 19.480 64.494 95.175 1.00 16.95 A ATOM810 O ALA A 108 19.442 63.899 94.098 1.00 16.28 A ATOM 811 N THR A 10919.412 65.820 95.269 1.00 15.93 A ATOM 812 CA THR A 109 19.309 66.64294.071 1.00 17.23 A ATOM 813 CB THR A 109 19.206 68.148 94.432 1.0017.73 A ATOM 814 OG1 THR A 109 17.994 68.381 95.160 1.00 16.64 A ATOM815 CG2 THR A 109 19.207 69.004 93.176 1.00 21.91 A ATOM 816 C THR A 10920.538 66.396 93.192 1.00 16.50 A ATOM 817 O THR A 109 20.430 66.29191.969 1.00 15.20 A ATOM 818 N LYS A 110 21.707 66.286 93.817 1.00 15.38A ATOM 819 CA LYS A 110 22.940 66.048 93.074 1.00 15.76 A ATOM 820 CBLYS A 110 24.149 66.168 94.002 1.00 16.69 A ATOM 821 CG LYS A 110 24.42867.571 94.486 1.00 19.70 A ATOM 822 CD LYS A 110 25.648 67.563 95.3841.00 20.65 A ATOM 823 CE LYS A 110 25.940 68.937 95.931 1.00 22.93 AATOM 824 NZ LYS A 110 27.124 68.891 96.839 1.00 21.69 A ATOM 825 C LYS A110 22.957 64.672 92.401 1.00 13.93 A ATOM 826 O LYS A 110 23.397 64.53091.257 1.00 13.99 A ATOM 827 N ALA A 111 22.482 63.659 93.115 1.00 15.58A ATOM 828 CA ALA A 111 22.449 62.306 92.561 1.00 14.44 A ATOM 829 CBALA A 111 22.046 61.318 93.640 1.00 14.66 A ATOM 830 C ALA A 111 21.46662.245 91.387 1.00 15.71 A ATOM 831 O ALA A 111 21.762 61.673 90.3381.00 14.80 A ATOM 832 N ILE A 112 20.297 62.851 91.560 1.00 16.78 A ATOM833 CA ILE A 112 19.298 62.851 90.499 1.00 17.55 A ATOM 834 CB ILE A 11217.973 63.474 90.993 1.00 17.59 A ATOM 835 CG2 ILE A 112 16.986 63.62089.837 1.00 17.13 A ATOM 836 CG1 ILE A 112 17.386 62.580 92.092 1.0020.85 A ATOM 837 CD1 ILE A 112 16.066 63.064 92.660 1.00 22.77 A ATOM838 C ILE A 112 19.828 63.586 89.268 1.00 18.57 A ATOM 839 O ILE A 11219.568 63.179 88.139 1.00 16.83 A ATOM 840 N LYS A 113 20.594 64.65189.484 1.00 19.85 A ATOM 841 CA LYS A 113 21.177 65.401 88.375 1.0021.93 A ATOM 842 CB LYS A 113 21.924 66.633 88.894 1.00 24.29 A ATOM 843CG LYS A 113 22.557 67.478 87.785 1.00 26.16 A ATOM 844 CD LYS A 11323.249 68.717 88.343 1.00 30.15 A ATOM 845 CE LYS A 113 23.865 69.54987.227 1.00 32.17 A ATOM 846 NZ LYS A 113 22.832 69.994 86.246 1.0033.78 A ATOM 847 C LYS A 113 22.141 64.515 87.576 1.00 22.24 A ATOM 848O LYS A 113 22.113 64.514 86.346 1.00 20.23 A ATOM 849 N GLU A 11422.994 63.763 88.274 1.00 20.31 A ATOM 850 CA GLU A 114 23.941 62.87287.603 1.00 20.76 A ATOM 851 CB GLU A 114 24.858 62.174 88.615 1.0020.34 A ATOM 852 CG GLU A 114 25.945 61.318 87.961 1.00 22.36 A ATOM 853CD GLU A 114 26.594 60.333 88.922 1.00 25.31 A ATOM 854 OE1 GLU A 11426.524 60.562 90.148 1.00 23.40 A ATOM 855 OE2 GLU A 114 27.188 59.33588.449 1.00 27.34 A ATOM 856 C GLU A 114 23.192 61.797 86.825 1.00 20.63A ATOM 857 O GLU A 114 23.520 61.506 85.677 1.00 20.09 A ATOM 858 N TRPA 115 22.197 61.206 87.483 1.00 19.11 A ATOM 859 CA TRP A 115 21.37360.148 86.912 1.00 19.80 A ATOM 860 CB TRP A 115 20.271 59.788 87.9091.00 16.70 A ATOM 861 CG TRP A 115 19.386 58.655 87.513 1.00 17.51 AATOM 862 CD2 TRP A 115 18.002 58.504 87.841 1.00 18.01 A ATOM 863 CE2TRP A 115 17.583 57.255 87.325 1.00 19.36 A ATOM 864 CE3 TRP A 11517.073 59.302 88.520 1.00 18.64 A ATOM 865 CD1 TRP A 115 19.744 57.52486.829 1.00 17.50 A ATOM 866 NE1 TRP A 115 18.666 56.679 86.714 1.0016.73 A ATOM 867 CZ2 TRP A 115 16.274 56.788 87.470 1.00 20.10 A ATOM868 CZ3 TRP A 115 15.769 58.837 88.663 1.00 18.36 A ATOM 869 CH2 TRP A115 15.384 57.589 88.139 1.00 19.75 A ATOM 870 C TRP A 115 20.786 60.61385.581 1.00 20.41 A ATOM 871 O TRP A 115 20.804 59.873 84.598 1.00 20.70A ATOM 872 N GLY A 116 20.278 61.844 85.560 1.00 20.64 A ATOM 873 CA GLYA 116 19.727 62.414 84.341 1.00 22.03 A ATOM 874 C GLY A 116 18.29762.044 83.998 1.00 22.10 A ATOM 875 O GLY A 116 17.767 62.487 82.9761.00 21.00 A ATOM 876 N GLN A 117 17.667 61.237 84.844 1.00 22.18 A ATOM877 CA GLN A 117 16.295 60.812 84.611 1.00 21.98 A ATOM 878 CB GLN A 11716.146 59.319 84.916 1.00 22.79 A ATOM 879 CG GLN A 117 16.986 58.42984.031 1.00 26.38 A ATOM 880 CD GLN A 117 16.533 58.474 82.589 1.0030.18 A ATOM 881 OE1 GLN A 117 15.401 58.104 82.273 1.00 34.37 A ATOM882 NE2 GLN A 117 17.409 58.933 81.708 1.00 31.61 A ATOM 883 C GLN A 11715.330 61.597 85.482 1.00 22.74 A ATOM 884 O GLN A 117 15.709 62.11686.538 1.00 20.98 A ATOM 885 N PRO A 118 14.063 61.698 85.049 1.00 22.98A ATOM 886 CD PRO A 118 13.555 61.274 83.735 1.00 24.02 A ATOM 887 CAPRO A 118 13.028 62.418 85.790 1.00 23.87 A ATOM 888 CB PRO A 118 11.80062.261 84.903 1.00 24.03 A ATOM 889 CG PRO A 118 12.382 62.200 83.5411.00 25.61 A ATOM 890 C PRO A 118 12.805 61.816 87.176 1.00 25.25 A ATOM891 O PRO A 118 12.820 60.595 87.351 1.00 23.22 A ATOM 892 N MET A 11912.596 62.694 88.145 1.00 24.78 A ATOM 893 CA MET A 119 12.354 62.32089.530 1.00 26.74 A ATOM 894 CB MET A 119 12.156 63.606 90.334 1.0029.70 A ATOM 895 CG MET A 119 11.815 63.454 91.789 1.00 32.65 A ATOM 896SD MET A 119 11.655 65.110 92.524 1.00 35.58 A ATOM 897 CE MET A 11910.351 65.815 91.532 1.00 38.18 A ATOM 898 C MET A 119 11.131 61.40089.638 1.00 25.23 A ATOM 899 O MET A 119 11.059 60.538 90.517 1.00 23.60A ATOM 900 N SER A 120 10.178 61.578 88.727 1.00 24.22 A ATOM 901 CA SERA 120 8.964 60.768 88.712 1.00 23.87 A ATOM 902 CB SER A 120 8.01561.275 87.618 1.00 25.63 A ATOM 903 OG SER A 120 8.630 61.217 86.3431.00 26.27 A ATOM 904 C SER A 120 9.247 59.277 88.492 1.00 22.48 A ATOM905 O SER A 120 8.394 58.432 88.762 1.00 21.93 A ATOM 906 N LYS A 12110.441 58.946 88.006 1.00 21.07 A ATOM 907 CA LYS A 121 10.770 57.53887.759 1.00 19.67 A ATOM 908 CB LYS A 121 11.766 57.421 86.606 1.0020.18 A ATOM 909 CG LYS A 121 11.291 58.113 85.333 1.00 22.53 A ATOM 910CD LYS A 121 12.096 57.675 84.121 1.00 26.21 A ATOM 911 CE LYS A 12111.351 56.608 83.328 1.00 29.93 A ATOM 912 NZ LYS A 121 10.074 57.12982.751 1.00 28.97 A ATOM 913 C LYS A 121 11.307 56.806 88.993 1.00 18.98A ATOM 914 O LYS A 121 11.593 55.604 88.935 1.00 18.06 A ATOM 915 N ILEA 122 11.451 57.532 90.099 1.00 17.26 A ATOM 916 CA ILE A 122 11.90956.936 91.352 1.00 15.68 A ATOM 917 CB ILE A 122 12.485 58.015 92.3211.00 16.42 A ATOM 918 CG2 ILE A 122 12.747 57.406 93.690 1.00 16.72 AATOM 919 CG1 ILE A 122 13.789 58.579 91.748 1.00 16.79 A ATOM 920 CD1ILE A 122 14.329 59.777 92.500 1.00 16.88 A ATOM 921 C ILE A 122 10.67956.263 91.962 1.00 15.84 A ATOM 922 O ILE A 122 9.640 56.900 92.173 1.0015.43 A ATOM 923 N THR A 123 10.796 54.966 92.226 1.00 14.18 A ATOM 924CA THR A 123 9.689 54.175 92.752 1.00 14.74 A ATOM 925 CB THR A 1239.549 52.891 91.934 1.00 16.36 A ATOM 926 OG1 THR A 123 10.802 52.19991.937 1.00 15.10 A ATOM 927 CG2 THR A 123 9.198 53.221 90.493 1.0017.32 A ATOM 928 C THR A 123 9.810 53.785 94.221 1.00 13.87 A ATOM 929 OTHR A 123 8.812 53.493 94.884 1.00 12.09 A ATOM 930 N HIS A 124 11.03253.769 94.725 1.00 12.46 A ATOM 931 CA HIS A 124 11.255 53.404 96.1141.00 13.52 A ATOM 932 CB HIS A 124 11.896 52.015 96.200 1.00 14.17 AATOM 933 CG HIS A 124 11.078 50.931 95.567 1.00 14.73 A ATOM 934 CD2 HISA 124 10.806 50.666 94.270 1.00 14.15 A ATOM 935 ND1 HIS A 124 10.44049.951 96.300 1.00 17.98 A ATOM 936 CE1 HIS A 124 9.812 49.128 95.4791.00 13.68 A ATOM 937 NE2 HIS A 124 10.019 49.539 94.241 1.00 18.64 AATOM 938 C HIS A 124 12.168 54.415 96.778 1.00 13.52 A ATOM 939 O HIS A124 13.081 54.952 96.147 1.00 15.74 A ATOM 940 N LEU A 125 11.921 54.66098.057 1.00 15.22 A ATOM 941 CA LEU A 125 12.737 55.586 98.826 1.0013.70 A ATOM 942 CB LEU A 125 11.969 56.874 99.138 1.00 12.90 A ATOM 943CG LEU A 125 12.658 57.787 100.168 1.00 14.85 A ATOM 944 CD1 LEU A 12513.951 58.355 99.576 1.00 13.04 A ATOM 945 CD2 LEU A 125 11.717 58.916100.575 1.00 13.73 A ATOM 946 C LEU A 125 13.159 54.966 100.143 1.0011.88 A ATOM 947 O LEU A 125 12.311 54.615 100.960 1.00 12.37 A ATOM 948N ILE A 126 14.466 54.837 100.340 1.00 11.11 A ATOM 949 CA ILE A 12615.008 54.328 101.598 1.00 11.89 A ATOM 950 CB ILE A 126 16.074 53.234101.380 1.00 11.91 A ATOM 951 CG2 ILE A 126 16.614 52.751 102.736 1.0014.16 A ATOM 952 CG1 ILE A 126 15.468 52.057 100.615 1.00 11.59 A ATOM953 CD1 ILE A 126 16.504 51.045 100.138 1.00 11.98 A ATOM 954 C ILE A126 15.691 55.518 102.274 1.00 12.26 A ATOM 955 O ILE A 126 16.63256.084 101.726 1.00 12.65 A ATOM 956 N PHE A 127 15.211 55.895 103.4531.00 10.80 A ATOM 957 CA PHE A 127 15.795 57.007 104.188 1.00 12.32 AATOM 958 CB PHE A 127 14.752 58.082 104.485 1.00 13.70 A ATOM 959 CG PHEA 127 15.353 59.410 104.858 1.00 16.44 A ATOM 960 CD1 PHE A 127 16.10059.550 106.025 1.00 19.42 A ATOM 961 CD2 PHE A 127 15.197 60.515 104.0251.00 18.87 A ATOM 962 CE1 PHE A 127 16.689 60.778 106.358 1.00 20.68 AATOM 963 CE2 PHE A 127 15.780 61.744 104.348 1.00 19.48 A ATOM 964 CZPHE A 127 16.525 61.875 105.514 1.00 19.21 A ATOM 965 C PHE A 127 16.35356.469 105.497 1.00 12.78 A ATOM 966 O PHE A 127 15.640 55.831 106.2781.00 14.15 A ATOM 967 N CYS A 128 17.626 56.748 105.737 1.00 13.01 AATOM 968 CA CYS A 128 18.301 56.259 106.930 1.00 13.64 A ATOM 969 CB CYSA 128 19.359 55.233 106.513 1.00 15.39 A ATOM 970 SG CYS A 128 20.37754.571 107.831 1.00 20.31 A ATOM 971 C CYS A 128 18.952 57.380 107.7141.00 15.17 A ATOM 972 O CYS A 128 19.726 58.159 107.161 1.00 14.59 AATOM 973 N THR A 129 18.622 57.466 108.999 1.00 14.32 A ATOM 974 CA THRA 129 19.205 58.482 109.868 1.00 16.20 A ATOM 975 CB THR A 129 18.47359.832 109.740 1.00 18.34 A ATOM 976 OG1 THR A 129 19.107 60.794 110.5961.00 18.62 A ATOM 977 CG2 THR A 129 17.006 59.692 110.122 1.00 14.76 AATOM 978 C THR A 129 19.174 58.022 111.324 1.00 16.46 A ATOM 979 O THR A129 18.273 57.287 111.731 1.00 17.28 A ATOM 980 N THR A 130 20.15858.463 112.102 1.00 18.56 A ATOM 981 CA THR A 130 20.263 58.082 113.5061.00 20.61 A ATOM 982 CB THR A 130 21.558 58.633 114.131 1.00 22.58 AATOM 983 OG1 THR A 130 22.683 57.978 113.531 1.00 24.26 A ATOM 984 CG2THR A 130 21.579 58.379 115.635 1.00 24.22 A ATOM 985 C THR A 130 19.07458.501 114.359 1.00 20.30 A ATOM 986 O THR A 130 18.636 57.741 115.2201.00 21.48 A ATOM 987 N SER A 131 18.552 59.703 114.140 1.00 20.01 AATOM 988 CA SER A 131 17.398 60.141 114.911 1.00 22.06 A ATOM 989 CB SERA 131 17.836 60.640 116.290 1.00 23.91 A ATOM 990 OG SER A 131 16.78760.471 117.229 1.00 24.77 A ATOM 991 C SER A 131 16.578 61.211 114.1891.00 22.16 A ATOM 992 O SER A 131 16.799 61.476 113.008 1.00 22.30 AATOM 993 N GLY A 132 15.633 61.817 114.906 1.00 22.15 A ATOM 994 CA GLYA 132 14.761 62.829 114.322 1.00 20.74 A ATOM 995 C GLY A 132 13.40362.167 114.193 1.00 19.96 A ATOM 996 O GLY A 132 12.845 62.049 113.1011.00 18.89 A ATOM 997 N VAL A 133 12.868 61.750 115.335 1.00 19.25 AATOM 998 CA VAL A 133 11.606 61.020 115.401 1.00 18.86 A ATOM 999 CB VALA 133 11.562 60.138 116.673 1.00 19.36 A ATOM 1000 CG1 VAL A 133 10.31659.272 116.662 1.00 20.48 A ATOM 1001 CG2 VAL A 133 12.815 59.288116.764 1.00 21.42 A ATOM 1002 C VAL A 133 10.307 61.810 115.343 1.0018.12 A ATOM 1003 O VAL A 133 9.972 62.554 116.257 1.00 15.85 A ATOM1004 N ALA A 134 9.566 61.603 114.260 1.00 17.33 A ATOM 1005 CA ALA A134 8.281 62.253 114.054 1.00 18.39 A ATOM 1006 CB ALA A 134 8.48063.600 113.376 1.00 18.75 A ATOM 1007 C ALA A 134 7.428 61.353 113.1701.00 20.02 A ATOM 1008 O ALA A 134 7.955 60.526 112.426 1.00 20.00 AATOM 1009 N LEU A 135 6.112 61.500 113.275 1.00 20.90 A ATOM 1010 CA LEUA 135 5.181 60.740 112.454 1.00 22.04 A ATOM 1011 CB LEU A 135 4.40159.715 113.284 1.00 22.48 A ATOM 1012 CG LEU A 135 5.190 58.568 113.9181.00 24.17 A ATOM 1013 CD1 LEU A 135 5.842 59.046 115.204 1.00 24.79 AATOM 1014 CD2 LEU A 135 4.254 57.399 114.203 1.00 25.37 A ATOM 1015 CLEU A 135 4.213 61.753 111.849 1.00 21.49 A ATOM 1016 O LEU A 135 3.49962.446 112.579 1.00 20.88 A ATOM 1017 N PRO A 136 4.212 61.887 110.5111.00 21.73 A ATOM 1018 CD PRO A 136 3.328 62.816 109.783 1.00 22.31 AATOM 1019 CA PRO A 136 5.063 61.143 109.576 1.00 22.02 A ATOM 1020 CBPRO A 136 4.528 61.570 108.209 1.00 21.01 A ATOM 1021 CG PRO A 136 4.04262.958 108.460 1.00 21.68 A ATOM 1022 C PRO A 136 6.541 61.479 109.7751.00 21.66 A ATOM 1023 O PRO A 136 6.877 62.527 110.326 1.00 20.41 AATOM 1024 N GLY A 137 7.412 60.582 109.326 1.00 21.85 A ATOM 1025 CA GLYA 137 8.843 60.771 109.499 1.00 22.07 A ATOM 1026 C GLY A 137 9.55561.689 108.528 1.00 21.47 A ATOM 1027 O GLY A 137 8.929 62.373 107.7111.00 20.25 A ATOM 1028 N VAL A 138 10.881 61.705 108.627 1.00 21.01 AATOM 1029 CA VAL A 138 11.693 62.538 107.758 1.00 21.43 A ATOM 1030 CBVAL A 138 13.150 62.616 108.258 1.00 21.99 A ATOM 1031 CG1 VAL A 13813.198 63.423 109.546 1.00 22.78 A ATOM 1032 CG2 VAL A 138 13.712 61.223108.483 1.00 20.43 A ATOM 1033 C VAL A 138 11.655 62.064 106.308 1.0020.81 A ATOM 1034 O VAL A 138 12.009 62.815 105.396 1.00 20.37 A ATOM1035 N ASP A 139 11.223 60.824 106.086 1.00 20.30 A ATOM 1036 CA ASP A139 11.116 60.324 104.719 1.00 20.26 A ATOM 1037 CB ASP A 139 10.77158.822 104.710 1.00 20.86 A ATOM 1038 CG ASP A 139 9.488 58.497 105.4651.00 21.95 A ATOM 1039 OD1 ASP A 139 9.282 59.048 106.568 1.00 21.43 AATOM 1040 OD2 ASP A 139 8.689 57.673 104.959 1.00 19.82 A ATOM 1041 CASP A 139 10.019 61.153 104.045 1.00 20.31 A ATOM 1042 O ASP A 13910.116 61.516 102.870 1.00 19.88 A ATOM 1043 N TYR A 140 8.981 61.465104.811 1.00 19.31 A ATOM 1044 CA TYR A 140 7.875 62.273 104.311 1.0020.68 A ATOM 1045 CB TYR A 140 6.746 62.317 105.346 1.00 22.10 A ATOM1046 CG TYR A 140 5.689 63.360 105.062 1.00 25.72 A ATOM 1047 CD1 TYR A140 4.629 63.093 104.196 1.00 24.85 A ATOM 1048 CE1 TYR A 140 3.66464.058 103.921 1.00 27.16 A ATOM 1049 CD2 TYR A 140 5.760 64.624 105.6461.00 26.43 A ATOM 1050 CE2 TYR A 140 4.804 65.596 105.374 1.00 28.31 AATOM 1051 CZ TYR A 140 3.758 65.306 104.512 1.00 27.72 A ATOM 1052 OHTYR A 140 2.812 66.265 104.241 1.00 30.75 A ATOM 1053 C TYR A 140 8.37863.692 104.034 1.00 21.06 A ATOM 1054 O TYR A 140 8.059 64.284 103.0071.00 21.05 A ATOM 1055 N GLU A 141 9.172 64.238 104.950 1.00 22.40 AATOM 1056 CA GLU A 141 9.697 65.587 104.766 1.00 23.04 A ATOM 1057 CBGLU A 141 10.550 65.990 105.973 1.00 25.22 A ATOM 1058 CG GLU A 1419.806 65.891 107.310 1.00 29.34 A ATOM 1059 CD GLU A 141 8.717 66.944107.473 1.00 32.95 A ATOM 1060 OE1 GLU A 141 7.895 66.815 108.407 1.0031.49 A ATOM 1061 OE2 GLU A 141 8.687 67.906 106.673 1.00 35.80 A ATOM1062 C GLU A 141 10.522 65.675 103.480 1.00 22.86 A ATOM 1063 O GLU A141 10.411 66.643 102.725 1.00 23.57 A ATOM 1064 N LEU A 142 11.34464.659 103.232 1.00 20.18 A ATOM 1065 CA LEU A 142 12.178 64.628 102.0331.00 19.91 A ATOM 1066 CB LEU A 142 13.115 63.412 102.057 1.00 18.95 AATOM 1067 CG LEU A 142 14.028 63.267 100.831 1.00 18.48 A ATOM 1068 CD1LEU A 142 15.022 64.433 100.771 1.00 16.40 A ATOM 1069 CD2 LEU A 14214.770 61.950 100.906 1.00 20.85 A ATOM 1070 C LEU A 142 11.305 64.579100.779 1.00 19.21 A ATOM 1071 O LEU A 142 11.585 65.260 99.796 1.0017.35 A ATOM 1072 N ILE A 143 10.246 63.773 100.821 1.00 17.49 A ATOM1073 CA ILE A 143 9.331 63.648 99.683 1.00 19.30 A ATOM 1074 CB ILE A143 8.175 62.680 100.010 1.00 19.22 A ATOM 1075 CG2 ILE A 143 7.06262.809 98.972 1.00 18.33 A ATOM 1076 CG1 ILE A 143 8.717 61.250 100.0771.00 19.66 A ATOM 1077 CD1 ILE A 143 7.730 60.236 100.615 1.00 22.67 AATOM 1078 C ILE A 143 8.755 65.019 99.327 1.00 20.59 A ATOM 1079 O ILE A143 8.663 65.382 98.152 1.00 20.63 A ATOM 1080 N VAL A 144 8.373 65.770100.353 1.00 21.01 A ATOM 1081 CA VAL A 144 7.818 67.102 100.165 1.0023.53 A ATOM 1082 CB VAL A 144 7.307 67.679 101.501 1.00 24.60 A ATOM1083 CG1 VAL A 144 6.932 69.145 101.329 1.00 27.88 A ATOM 1084 CG2 VAL A144 6.111 66.883 101.979 1.00 26.36 A ATOM 1085 C VAL A 144 8.860 68.05599.590 1.00 22.64 A ATOM 1086 O VAL A 144 8.578 68.805 98.660 1.00 21.65A ATOM 1087 N LEU A 145 10.069 68.015 100.141 1.00 23.18 A ATOM 1088 CALEU A 145 11.142 68.894 99.685 1.00 24.35 A ATOM 1089 CB LEU A 14512.331 68.823 100.644 1.00 25.00 A ATOM 1090 CG LEU A 145 12.167 69.569101.968 1.00 25.62 A ATOM 1091 CD1 LEU A 145 13.325 69.229 102.901 1.0025.97 A ATOM 1092 CD2 LEU A 145 12.109 71.071 101.703 1.00 27.80 A ATOM1093 C LEU A 145 11.624 68.627 98.270 1.00 25.21 A ATOM 1094 O LEU A 14511.994 69.563 97.562 1.00 25.41 A ATOM 1095 N LEU A 146 11.628 67.36097.860 1.00 24.69 A ATOM 1096 CA LEU A 146 12.074 66.988 96.519 1.0023.80 A ATOM 1097 CB LEU A 146 12.652 65.571 96.506 1.00 24.17 A ATOM1098 CG LEU A 146 14.086 65.321 96.952 1.00 22.03 A ATOM 1099 CD1 LEU A146 14.373 63.824 96.883 1.00 20.90 A ATOM 1100 CD2 LEU A 146 15.04866.100 96.055 1.00 24.88 A ATOM 1101 C LEU A 146 10.958 67.037 95.4951.00 24.42 A ATOM 1102 O LEU A 146 11.162 67.482 94.366 1.00 26.11 AATOM 1103 N GLY A 147 9.787 66.550 95.890 1.00 23.14 A ATOM 1104 CA GLYA 147 8.655 66.515 94.985 1.00 22.12 A ATOM 1105 C GLY A 147 8.49465.121 94.405 1.00 21.57 A ATOM 1106 O GLY A 147 8.049 64.965 93.2681.00 21.52 A ATOM 1107 N LEU A 148 8.874 64.107 95.183 1.00 20.27 A ATOM1108 CA LEU A 148 8.757 62.711 94.759 1.00 21.34 A ATOM 1109 CB LEU A148 9.387 61.777 95.802 1.00 20.35 A ATOM 1110 CG LEU A 148 10.90961.838 95.961 1.00 22.06 A ATOM 1111 CD1 LEU A 148 11.357 60.867 97.0371.00 21.03 A ATOM 1112 CD2 LEU A 148 11.571 61.512 94.625 1.00 21.84 AATOM 1113 C LEU A 148 7.291 62.336 94.577 1.00 20.24 A ATOM 1114 O LEU A148 6.408 62.970 95.150 1.00 19.49 A ATOM 1115 N ASP A 149 7.035 61.30393.779 1.00 21.19 A ATOM 1116 CA ASP A 149 5.669 60.854 93.526 1.0020.81 A ATOM 1117 CB ASP A 149 5.678 59.672 92.550 1.00 23.34 A ATOM1118 CG ASP A 149 4.286 59.342 92.019 1.00 25.67 A ATOM 1119 OD1 ASP A149 3.482 58.732 92.757 1.00 23.21 A ATOM 1120 OD2 ASP A 149 3.99159.715 90.863 1.00 28.37 A ATOM 1121 C ASP A 149 5.007 60.436 94.8371.00 21.87 A ATOM 1122 O ASP A 149 5.628 59.759 95.672 1.00 22.11 A ATOM1123 N PRO A 150 3.741 60.834 95.044 1.00 19.56 A ATOM 1124 CD PRO A 1502.883 61.659 94.177 1.00 21.27 A ATOM 1125 CA PRO A 150 3.037 60.47296.278 1.00 19.66 A ATOM 1126 CB PRO A 150 1.696 61.199 96.141 1.0020.41 A ATOM 1127 CG PRO A 150 1.498 61.272 94.651 1.00 22.21 A ATOM1128 C PRO A 150 2.880 58.961 96.448 1.00 18.44 A ATOM 1129 O PRO A 1502.565 58.480 97.539 1.00 18.21 A ATOM 1130 N CYS A 151 3.110 58.21795.371 1.00 17.66 A ATOM 1131 CA CYS A 151 3.000 56.762 95.425 1.0018.31 A ATOM 1132 CB CYS A 151 2.269 56.241 94.190 1.00 19.55 A ATOM1133 SG CYS A 151 .546 56.775 94.144 1.00 24.40 A ATOM 1134 C CYS A 1514.349 56.073 95.561 1.00 17.28 A ATOM 1135 O CYS A 151 4.465 54.86295.353 1.00 16.35 A ATOM 1136 N VAL A 152 5.377 56.837 95.913 1.00 16.24A ATOM 1137 CA VAL A 152 6.700 56.247 96.086 1.00 15.84 A ATOM 1138 CBVAL A 152 7.764 57.336 96.339 1.00 15.86 A ATOM 1139 CG1 VAL A 152 7.48958.033 97.667 1.00 18.85 A ATOM 1140 CG2 VAL A 152 9.159 56.726 96.3231.00 16.14 A ATOM 1141 C VAL A 152 6.632 55.308 97.302 1.00 16.12 A ATOM1142 O VAL A 152 5.989 55.630 98.302 1.00 16.07 A ATOM 1143 N LYS A 1537.264 54.140 97.208 1.00 15.09 A ATOM 1144 CA LYS A 153 7.268 53.19698.325 1.00 15.78 A ATOM 1145 CB LYS A 153 7.422 51.764 97.810 1.0015.41 A ATOM 1146 CG LYS A 153 6.190 51.244 97.072 1.00 18.15 A ATOM1147 CD LYS A 153 6.434 49.827 96.560 1.00 21.61 A ATOM 1148 CE LYS A153 5.205 49.245 95.886 1.00 24.97 A ATOM 1149 NZ LYS A 153 4.778 50.04994.708 1.00 28.12 A ATOM 1150 C LYS A 153 8.405 53.551 99.291 1.00 14.03A ATOM 1151 O LYS A 153 9.573 53.586 98.909 1.00 14.56 A ATOM 1152 N ARGA 154 8.047 53.803 100.546 1.00 14.71 A ATOM 1153 CA ARG A 154 9.01454.215 101.559 1.00 14.98 A ATOM 1154 CB ARG A 154 8.448 55.402 102.3461.00 15.82 A ATOM 1155 CG ARG A 154 8.113 56.614 101.492 1.00 16.52 AATOM 1156 CD ARG A 154 6.666 57.044 101.681 1.00 19.72 A ATOM 1157 NEARG A 154 6.382 57.386 103.070 1.00 19.17 A ATOM 1158 CZ ARG A 154 5.15857.536 103.566 1.00 22.61 A ATOM 1159 NH1 ARG A 154 4.097 57.379 102.7861.00 22.37 A ATOM 1160 NH2 ARG A 154 4.992 57.826 104.848 1.00 24.78 AATOM 1161 C ARG A 154 9.493 53.170 102.565 1.00 14.29 A ATOM 1162 O ARGA 154 8.757 52.274 102.961 1.00 12.71 A ATOM 1163 N TYR A 155 10.74653.329 102.983 1.00 14.99 A ATOM 1164 CA TYR A 155 11.375 52.466 103.9721.00 15.35 A ATOM 1165 CB TYR A 155 12.312 51.462 103.283 1.00 15.70 AATOM 1166 CG TYR A 155 11.596 50.631 102.228 1.00 15.84 A ATOM 1167 CD1TYR A 155 11.282 51.176 100.985 1.00 16.66 A ATOM 1168 CE1 TYR A 15510.528 50.467 100.051 1.00 16.19 A ATOM 1169 CD2 TYR A 155 11.144 49.338102.511 1.00 16.71 A ATOM 1170 CE2 TYR A 155 10.388 48.613 101.581 1.0017.09 A ATOM 1171 CZ TYR A 155 10.078 49.189 100.355 1.00 17.25 A ATOM1172 OH TYR A 155 9.283 48.526 99.447 1.00 15.92 A ATOM 1173 C TYR A 15512.148 53.425 104.882 1.00 14.71 A ATOM 1174 O TYR A 155 13.241 53.869104.546 1.00 14.74 A ATOM 1175 N MET A 156 11.550 53.752 106.022 1.0014.82 A ATOM 1176 CA MET A 156 12.134 54.679 106.992 1.00 17.67 A ATOM1177 CB MET A 156 10.997 55.466 107.663 1.00 19.67 A ATOM 1178 CG MET A156 11.412 56.537 108.663 1.00 20.86 A ATOM 1179 SD MET A 156 12.37057.875 107.942 1.00 19.21 A ATOM 1180 CE MET A 156 13.973 57.560 108.7041.00 20.63 A ATOM 1181 C MET A 156 12.963 53.915 108.027 1.00 17.40 AATOM 1182 O MET A 156 12.421 53.225 108.896 1.00 16.91 A ATOM 1183 N META 157 14.279 54.050 107.927 1.00 17.80 A ATOM 1184 CA MET A 157 15.19953.363 108.828 1.00 18.64 A ATOM 1185 CB MET A 157 16.338 52.745 108.0081.00 18.72 A ATOM 1186 CG MET A 157 15.867 52.052 106.719 1.00 20.59 AATOM 1187 SD MET A 157 14.560 50.808 106.973 1.00 23.41 A ATOM 1188 CEMET A 157 15.566 49.431 107.583 1.00 23.66 A ATOM 1189 C MET A 15715.769 54.291 109.911 1.00 20.02 A ATOM 1190 O MET A 157 16.658 55.108109.647 1.00 17.80 A ATOM 1191 N TYR A 158 15.253 54.156 111.131 1.0019.95 A ATOM 1192 CA TYR A 158 15.695 54.972 112.256 1.00 19.35 A ATOM1193 CB TYR A 158 14.483 55.463 113.064 1.00 19.50 A ATOM 1194 CG TYR A158 13.763 56.698 112.550 1.00 20.57 A ATOM 1195 CD1 TYR A 158 14.39757.942 112.528 1.00 18.96 A ATOM 1196 CE1 TYR A 158 13.713 59.097112.154 1.00 19.96 A ATOM 1197 CD2 TYR A 158 12.418 56.641 112.173 1.0019.97 A ATOM 1198 CE2 TYR A 158 11.723 57.801 111.797 1.00 21.41 A ATOM1199 CZ TYR A 158 12.379 59.024 111.794 1.00 21.79 A ATOM 1200 OH TYR A158 11.703 60.185 111.455 1.00 21.85 A ATOM 1201 C TYR A 158 16.62254.198 113.210 1.00 20.02 A ATOM 1202 O TYR A 158 16.527 52.974 113.3401.00 19.80 A ATOM 1203 N HIS A 159 17.518 54.925 113.872 1.00 19.60 AATOM 1204 CA HIS A 159 18.422 54.340 114.863 1.00 20.67 A ATOM 1205 CBHIS A 159 17.648 54.094 116.157 1.00 21.27 A ATOM 1206 CG HIS A 15916.600 55.123 116.445 1.00 22.15 A ATOM 1207 CD2 HIS A 159 15.253 55.021116.534 1.00 21.57 A ATOM 1208 ND1 HIS A 159 16.902 56.444 116.699 1.0022.61 A ATOM 1209 CE1 HIS A 159 15.785 57.110 116.934 1.00 22.64 A ATOM1210 NE2 HIS A 159 14.771 56.270 116.841 1.00 24.23 A ATOM 1211 C HIS A159 19.062 53.023 114.436 1.00 23.07 A ATOM 1212 O HIS A 159 19.09252.069 115.218 1.00 23.59 A ATOM 1213 N GLN A 160 19.584 52.970 113.2181.00 22.10 A ATOM 1214 CA GLN A 160 20.190 51.746 112.703 1.00 25.43 AATOM 1215 CB GLN A 160 20.173 51.759 111.175 1.00 24.14 A ATOM 1216 CGGLN A 160 18.831 52.116 110.568 1.00 26.85 A ATOM 1217 CD GLN A 16017.869 50.948 110.516 1.00 28.45 A ATOM 1218 OE1 GLN A 160 18.111 49.964109.811 1.00 28.85 A ATOM 1219 NE2 GLN A 160 16.767 51.049 111.256 1.0025.36 A ATOM 1220 C GLN A 160 21.620 51.550 113.181 1.00 26.36 A ATOM1221 O GLN A 160 22.037 50.431 113.465 1.00 30.01 A ATOM 1222 N GLY A161 22.377 52.637 113.257 1.00 26.59 A ATOM 1223 CA GLY A 161 23.75452.524 113.691 1.00 26.91 A ATOM 1224 C GLY A 161 24.746 52.665 112.5491.00 26.02 A ATOM 1225 O GLY A 161 24.369 52.731 111.374 1.00 25.41 AATOM 1226 N CYS A 162 26.026 52.682 112.904 1.00 22.86 A ATOM 1227 CACYS A 162 27.108 52.848 111.942 1.00 21.74 A ATOM 1228 CB CYS A 16228.428 53.028 112.698 1.00 24.49 A ATOM 1229 SG CYS A 162 28.529 54.618113.582 1.00 31.19 A ATOM 1230 C CYS A 162 27.282 51.787 110.855 1.0019.91 A ATOM 1231 O CYS A 162 28.078 51.979 109.941 1.00 19.35 A ATOM1232 N PHE A 163 26.561 50.673 110.940 1.00 17.83 A ATOM 1233 CA PHE A163 26.692 49.640 109.914 1.00 19.23 A ATOM 1234 CB PHE A 163 26.62148.239 110.544 1.00 19.59 A ATOM 1235 CG PHE A 163 25.314 47.939 111.2391.00 19.53 A ATOM 1236 CD1 PHE A 163 24.135 47.796 110.513 1.00 19.57 AATOM 1237 CD2 PHE A 163 25.264 47.817 112.626 1.00 21.14 A ATOM 1238 CE1PHE A 163 22.924 47.539 111.156 1.00 19.62 A ATOM 1239 CE2 PHE A 16324.061 47.559 113.279 1.00 20.54 A ATOM 1240 CZ PHE A 163 22.889 47.421112.542 1.00 24.00 A ATOM 1241 C PHE A 163 25.606 49.775 108.846 1.0018.82 A ATOM 1242 O PHE A 163 25.630 49.077 107.829 1.00 19.22 A ATOM1243 N ALA A 164 24.663 50.679 109.088 1.00 16.89 A ATOM 1244 CA ALA A164 23.534 50.900 108.186 1.00 17.06 A ATOM 1245 CB ALA A 164 22.66352.040 108.710 1.00 18.50 A ATOM 1246 C ALA A 164 23.877 51.142 106.7241.00 16.53 A ATOM 1247 O ALA A 164 23.015 50.985 105.859 1.00 18.01 AATOM 1248 N GLY A 165 25.115 51.543 106.443 1.00 15.99 A ATOM 1249 CAGLY A 165 25.521 51.758 105.064 1.00 16.79 A ATOM 1250 C GLY A 16525.337 50.452 104.309 1.00 18.19 A ATOM 1251 O GLY A 165 24.874 50.420103.160 1.00 19.45 A ATOM 1252 N GLY A 166 25.700 49.358 104.965 1.0018.25 A ATOM 1253 CA GLY A 166 25.531 48.056 104.352 1.00 17.94 A ATOM1254 C GLY A 166 24.063 47.644 104.344 1.00 17.15 A ATOM 1255 O GLY A166 23.597 47.031 103.384 1.00 18.05 A ATOM 1256 N THR A 167 23.33947.988 105.408 1.00 17.80 A ATOM 1257 CA THR A 167 21.921 47.647 105.5451.00 17.61 A ATOM 1258 CB THR A 167 21.331 48.188 106.866 1.00 20.13 AATOM 1259 OG1 THR A 167 22.114 47.730 107.978 1.00 22.66 A ATOM 1260 CG2THR A 167 19.896 47.709 107.040 1.00 20.30 A ATOM 1261 C THR A 16721.076 48.208 104.400 1.00 16.77 A ATOM 1262 O THR A 167 20.233 47.504103.837 1.00 14.42 A ATOM 1263 N VAL A 168 21.295 49.473 104.050 1.0014.03 A ATOM 1264 CA VAL A 168 20.512 50.071 102.974 1.00 13.42 A ATOM1265 CB VAL A 168 20.710 51.608 102.899 1.00 13.78 A ATOM 1266 CG1 VAL A168 20.145 52.250 104.155 1.00 13.71 A ATOM 1267 CG2 VAL A 168 22.18351.955 102.740 1.00 15.67 A ATOM 1268 C VAL A 168 20.804 49.438 101.6201.00 13.51 A ATOM 1269 O VAL A 168 19.898 49.307 100.800 1.00 15.08 AATOM 1270 N LEU A 169 22.054 49.037 101.379 1.00 13.10 A ATOM 1271 CALEU A 169 22.397 48.397 100.107 1.00 14.82 A ATOM 1272 CB LEU A 16923.920 48.257 99.954 1.00 15.02 A ATOM 1273 CG LEU A 169 24.672 49.55999.643 1.00 15.90 A ATOM 1274 CD1 LEU A 169 26.175 49.323 99.692 1.0018.49 A ATOM 1275 CD2 LEU A 169 24.259 50.063 98.272 1.00 16.52 A ATOM1276 C LEU A 169 21.731 47.021 100.059 1.00 14.69 A ATOM 1277 O LEU A169 21.208 46.609 99.019 1.00 14.57 A ATOM 1278 N ARG A 170 21.74346.323 101.194 1.00 14.14 A ATOM 1279 CA ARG A 170 21.123 45.003 101.3091.00 13.98 A ATOM 1280 CB ARG A 170 21.363 44.457 102.727 1.00 18.76 AATOM 1281 CG ARG A 170 20.615 43.185 103.107 1.00 18.37 A ATOM 1282 CDARG A 170 21.288 42.496 104.306 1.00 18.20 A ATOM 1283 NE ARG A 17021.420 43.343 105.500 1.00 18.43 A ATOM 1284 CZ ARG A 170 20.434 43.602106.355 1.00 18.99 A ATOM 1285 NH1 ARG A 170 19.231 43.082 106.159 1.0015.93 A ATOM 1286 NH2 ARG A 170 20.650 44.378 107.415 1.00 18.98 A ATOM1287 C ARG A 170 19.626 45.116 101.006 1.00 15.04 A ATOM 1288 O ARG A170 19.045 44.266 100.325 1.00 13.87 A ATOM 1289 N LEU A 171 19.01046.185 101.496 1.00 14.48 A ATOM 1290 CA LEU A 171 17.588 46.412 101.2691.00 16.01 A ATOM 1291 CB LEU A 171 17.066 47.488 102.229 1.00 16.51 AATOM 1292 CG LEU A 171 15.657 48.037 101.983 1.00 18.42 A ATOM 1293 CD1LEU A 171 14.644 46.910 101.951 1.00 19.05 A ATOM 1294 CD2 LEU A 17115.305 49.032 103.076 1.00 17.79 A ATOM 1295 C LEU A 171 17.323 46.83499.823 1.00 15.61 A ATOM 1296 O LEU A 171 16.413 46.313 99.174 1.0016.14 A ATOM 1297 N ALA A 172 18.116 47.775 99.314 1.00 15.72 A ATOM1298 CA ALA A 172 17.934 48.241 97.942 1.00 15.52 A ATOM 1299 CB ALA A172 18.911 49.378 97.636 1.00 17.06 A ATOM 1300 C ALA A 172 18.10947.115 96.923 1.00 15.78 A ATOM 1301 O ALA A 172 17.430 47.083 95.8961.00 14.10 A ATOM 1302 N LYS A 173 19.008 46.184 97.211 1.00 15.48 AATOM 1303 CA LYS A 173 19.251 45.083 96.288 1.00 15.99 A ATOM 1304 CBLYS A 173 20.325 44.148 96.851 1.00 15.75 A ATOM 1305 CG LYS A 17320.576 42.910 96.001 1.00 16.03 A ATOM 1306 CD LYS A 173 21.788 42.14796.512 1.00 19.74 A ATOM 1307 CE LYS A 173 21.600 40.640 96.392 1.0022.75 A ATOM 1308 NZ LYS A 173 21.274 40.183 95.023 1.00 21.00 A ATOM1309 C LYS A 173 17.985 44.289 95.972 1.00 16.47 A ATOM 1310 O LYS A 17317.703 44.008 94.804 1.00 16.32 A ATOM 1311 N ASP A 174 17.230 43.92497.005 1.00 15.20 A ATOM 1312 CA ASP A 174 16.006 43.158 96.804 1.0017.12 A ATOM 1313 CB ASP A 174 15.496 42.574 98.126 1.00 18.01 A ATOM1314 CG ASP A 174 16.319 41.378 98.597 1.00 21.22 A ATOM 1315 OD1 ASP A174 16.943 40.698 97.752 1.00 23.11 A ATOM 1316 OD2 ASP A 174 16.32341.103 99.814 1.00 19.95 A ATOM 1317 C ASP A 174 14.909 43.988 96.1491.00 15.70 A ATOM 1318 O ASP A 174 14.155 43.479 95.318 1.00 14.62 AATOM 1319 N LEU A 175 14.814 45.263 96.522 1.00 14.64 A ATOM 1320 CA LEUA 175 13.804 46.138 95.936 1.00 16.58 A ATOM 1321 CB LEU A 175 13.84147.529 96.592 1.00 16.05 A ATOM 1322 CG LEU A 175 13.445 47.613 98.0701.00 16.89 A ATOM 1323 CD1 LEU A 175 13.483 49.061 98.527 1.00 16.97 AATOM 1324 CD2 LEU A 175 12.060 47.041 98.269 1.00 17.52 A ATOM 1325 CLEU A 175 14.015 46.298 94.430 1.00 15.43 A ATOM 1326 O LEU A 175 13.07346.163 93.642 1.00 17.97 A ATOM 1327 N ALA A 176 15.246 46.589 94.0211.00 14.64 A ATOM 1328 CA ALA A 176 15.529 46.777 92.601 1.00 14.54 AATOM 1329 CB ALA A 176 16.918 47.382 92.412 1.00 16.05 A ATOM 1330 C ALAA 176 15.421 45.508 91.764 1.00 15.09 A ATOM 1331 O ALA A 176 14.92345.536 90.637 1.00 13.49 A ATOM 1332 N GLU A 177 15.899 44.398 92.3091.00 14.74 A ATOM 1333 CA GLU A 177 15.898 43.143 91.571 1.00 16.33 AATOM 1334 CB GLU A 177 16.949 42.196 92.170 1.00 16.12 A ATOM 1335 CGGLU A 177 18.370 42.756 92.074 1.00 17.28 A ATOM 1336 CD GLU A 17719.425 41.845 92.680 1.00 18.83 A ATOM 1337 OE1 GLU A 177 19.056 40.93893.457 1.00 16.57 A ATOM 1338 OE2 GLU A 177 20.624 42.051 92.388 1.0016.51 A ATOM 1339 C GLU A 177 14.568 42.422 91.445 1.00 15.11 A ATOM1340 O GLU A 177 14.355 41.688 90.479 1.00 16.69 A ATOM 1341 N ASN A 17813.667 42.633 92.398 1.00 15.01 A ATOM 1342 CA ASN A 178 12.387 41.94592.370 1.00 16.15 A ATOM 1343 CB ASN A 178 11.944 41.597 93.793 1.0014.81 A ATOM 1344 CG ASN A 178 10.875 40.519 93.815 1.00 18.14 A ATOM1345 OD1 ASN A 178 11.012 39.493 93.148 1.00 14.61 A ATOM 1346 ND2 ASN A178 9.813 40.743 94.578 1.00 16.87 A ATOM 1347 C ASN A 178 11.279 42.72691.677 1.00 17.15 A ATOM 1348 O ASN A 178 10.161 42.233 91.550 1.0015.08 A ATOM 1349 N ASN A 179 11.594 43.932 91.215 1.00 17.66 A ATOM1350 CA ASN A 179 10.595 44.773 90.568 1.00 18.39 A ATOM 1351 CB ASN A179 10.162 45.870 91.545 1.00 19.49 A ATOM 1352 CG ASN A 179 9.50545.303 92.787 1.00 18.74 A ATOM 1353 OD1 ASN A 179 8.377 44.818 92.7341.00 19.10 A ATOM 1354 ND2 ASN A 179 10.216 45.341 93.909 1.00 19.12 AATOM 1355 C ASN A 179 11.069 45.393 89.262 1.00 18.82 A ATOM 1356 O ASNA 179 11.957 46.248 89.251 1.00 18.76 A ATOM 1357 N LYS A 180 10.46944.960 88.157 1.00 18.18 A ATOM 1358 CA LYS A 180 10.841 45.484 86.8561.00 17.68 A ATOM 1359 CB LYS A 180 9.980 44.851 85.759 1.00 19.83 AATOM 1360 CG LYS A 180 10.364 45.309 84.357 1.00 22.78 A ATOM 1361 CDLYS A 180 9.565 44.576 83.284 1.00 28.75 A ATOM 1362 CE LYS A 180 9.92245.066 81.883 1.00 29.71 A ATOM 1363 NZ LYS A 180 11.333 44.765 81.5001.00 32.99 A ATOM 1364 C LYS A 180 10.686 47.005 86.833 1.00 16.88 AATOM 1365 O LYS A 180 9.668 47.541 87.268 1.00 15.93 A ATOM 1366 N ASP A181 11.725 47.684 86.355 1.00 18.30 A ATOM 1367 CA ASP A 181 11.75549.144 86.243 1.00 20.40 A ATOM 1368 CB ASP A 181 10.514 49.645 85.4961.00 22.88 A ATOM 1369 CG ASP A 181 10.441 49.128 84.070 1.00 25.36 AATOM 1370 OD1 ASP A 181 11.469 49.186 83.369 1.00 27.75 A ATOM 1371 OD2ASP A 181 9.354 48.677 83.647 1.00 28.77 A ATOM 1372 C ASP A 181 11.88649.907 87.561 1.00 19.53 A ATOM 1373 O ASP A 181 11.843 51.140 87.5721.00 20.09 A ATOM 1374 N ALA A 182 12.055 49.195 88.668 1.00 17.14 AATOM 1375 CA ALA A 182 12.181 49.873 89.950 1.00 16.34 A ATOM 1376 CBALA A 182 12.174 48.858 91.094 1.00 16.60 A ATOM 1377 C ALA A 182 13.46350.694 90.000 1.00 14.49 A ATOM 1378 O ALA A 182 14.517 50.241 89.5671.00 13.96 A ATOM 1379 N ARG A 183 13.357 51.916 90.510 1.00 14.46 AATOM 1380 CA ARG A 183 14.516 52.788 90.668 1.00 15.12 A ATOM 1381 CBARG A 183 14.474 53.953 89.679 1.00 14.27 A ATOM 1382 CG ARG A 18314.834 53.538 88.266 1.00 14.93 A ATOM 1383 CD ARG A 183 16.287 53.08488.169 1.00 13.32 A ATOM 1384 NE ARG A 183 16.653 52.650 86.819 1.0016.28 A ATOM 1385 CZ ARG A 183 16.497 51.413 86.349 1.00 17.08 A ATOM1386 NH1 ARG A 183 15.975 50.459 87.112 1.00 15.62 A ATOM 1387 NH2 ARG A183 16.892 51.118 85.119 1.00 19.64 A ATOM 1388 C ARG A 183 14.44653.273 92.104 1.00 14.84 A ATOM 1389 O ARG A 183 13.512 53.989 92.4951.00 13.87 A ATOM 1390 N VAL A 184 15.435 52.851 92.886 1.00 13.98 AATOM 1391 CA VAL A 184 15.500 53.157 94.313 1.00 13.66 A ATOM 1392 CBVAL A 184 15.984 51.919 95.105 1.00 12.76 A ATOM 1393 CG1 VAL A 18415.823 52.141 96.617 1.00 13.61 A ATOM 1394 CG2 VAL A 184 15.224 50.69394.651 1.00 14.50 A ATOM 1395 C VAL A 184 16.413 54.322 94.663 1.0013.84 A ATOM 1396 O VAL A 184 17.550 54.395 94.202 1.00 15.51 A ATOM1397 N LEU A 185 15.894 55.236 95.475 1.00 12.87 A ATOM 1398 CA LEU A185 16.672 56.375 95.931 1.00 12.68 A ATOM 1399 CB LEU A 185 15.86157.679 95.834 1.00 11.22 A ATOM 1400 CG LEU A 185 16.532 58.905 96.4661.00 11.54 A ATOM 1401 CD1 LEU A 185 17.866 59.176 95.778 1.00 13.85 AATOM 1402 CD2 LEU A 185 15.612 60.122 96.370 1.00 11.09 A ATOM 1403 CLEU A 185 17.017 56.106 97.394 1.00 11.63 A ATOM 1404 O LEU A 185 16.12755.958 98.230 1.00 13.09 A ATOM 1405 N ILE A 186 18.305 56.010 97.6951.00 12.57 A ATOM 1406 CA ILE A 186 18.721 55.803 99.072 1.00 12.90 AATOM 1407 CB ILE A 186 19.867 54.790 99.209 1.00 12.53 A ATOM 1408 CG2ILE A 186 20.293 54.706 100.672 1.00 15.79 A ATOM 1409 CG1 ILE A 18619.441 53.411 98.703 1.00 17.58 A ATOM 1410 CD1 ILE A 186 20.562 52.37298.791 1.00 15.67 A ATOM 1411 C ILE A 186 19.265 57.126 99.580 1.0012.87 A ATOM 1412 O ILE A 186 20.041 57.782 98.899 1.00 12.60 A ATOM1413 N VAL A 187 18.851 57.515 100.776 1.00 13.22 A ATOM 1414 CA VAL A187 19.359 58.741 101.361 1.00 13.67 A ATOM 1415 CB VAL A 187 18.31659.866 101.349 1.00 14.26 A ATOM 1416 CG1 VAL A 187 18.866 61.083102.088 1.00 15.07 A ATOM 1417 CG2 VAL A 187 17.967 60.228 99.917 1.0017.12 A ATOM 1418 C VAL A 187 19.763 58.463 102.795 1.00 11.28 A ATOM1419 O VAL A 187 18.930 58.089 103.618 1.00 12.82 A ATOM 1420 N CYS A188 21.051 58.621 103.071 1.00 13.30 A ATOM 1421 CA CYS A 188 21.60958.430 104.410 1.00 13.30 A ATOM 1422 CB CYS A 188 22.816 57.490 104.3821.00 14.21 A ATOM 1423 SG CYS A 188 22.413 55.739 104.060 1.00 17.94 AATOM 1424 C CYS A 188 22.058 59.817 104.839 1.00 11.22 A ATOM 1425 O CYSA 188 22.938 60.401 104.220 1.00 13.60 A ATOM 1426 N SER A 189 21.45260.332 105.899 1.00 12.04 A ATOM 1427 CA SER A 189 21.765 61.675 106.3771.00 12.31 A ATOM 1428 CB SER A 189 20.612 62.615 106.024 1.00 14.07 AATOM 1429 OG SER A 189 20.919 63.953 106.369 1.00 13.79 A ATOM 1430 CSER A 189 21.976 61.646 107.882 1.00 11.93 A ATOM 1431 O SER A 18921.054 61.336 108.638 1.00 13.29 A ATOM 1432 N GLU A 190 23.185 61.993108.314 1.00 14.10 A ATOM 1433 CA GLU A 190 23.530 61.959 109.734 1.0013.97 A ATOM 1434 CB GLU A 190 24.692 60.989 109.951 1.00 16.13 A ATOM1435 CG GLU A 190 24.461 59.577 109.378 1.00 17.69 A ATOM 1436 CD GLU A190 23.440 58.747 110.160 1.00 20.46 A ATOM 1437 OE1 GLU A 190 22.98459.185 111.237 1.00 17.84 A ATOM 1438 OE2 GLU A 190 23.096 57.638109.692 1.00 22.18 A ATOM 1439 C GLU A 190 23.890 63.345 110.270 1.0014.72 A ATOM 1440 O GLU A 190 24.438 64.184 109.551 1.00 13.22 A ATOM1441 N ASN A 191 23.584 63.569 111.542 1.00 14.47 A ATOM 1442 CA ASN A191 23.826 64.860 112.174 1.00 16.59 A ATOM 1443 CB ASN A 191 22.57765.726 111.979 1.00 15.33 A ATOM 1444 CG ASN A 191 22.778 67.164 112.4051.00 16.18 A ATOM 1445 OD1 ASN A 191 23.151 67.441 113.540 1.00 16.84 AATOM 1446 ND2 ASN A 191 22.505 68.094 111.492 1.00 16.25 A ATOM 1447 CASN A 191 24.113 64.643 113.665 1.00 17.21 A ATOM 1448 O ASN A 19123.396 63.894 114.334 1.00 16.87 A ATOM 1449 N THR A 192 25.141 65.310114.187 1.00 17.46 A ATOM 1450 CA THR A 192 25.527 65.144 115.594 1.0017.77 A ATOM 1451 CB THR A 192 27.025 65.466 115.792 1.00 19.46 A ATOM1452 OG1 THR A 192 27.302 66.792 115.326 1.00 21.72 A ATOM 1453 CG2 THRA 192 27.885 64.475 115.021 1.00 24.93 A ATOM 1454 C THR A 192 24.71965.923 116.637 1.00 17.73 A ATOM 1455 O THR A 192 25.014 65.861 117.8351.00 17.54 A ATOM 1456 N ALA A 193 23.693 66.643 116.199 1.00 16.98 AATOM 1457 CA ALA A 193 22.872 67.407 117.131 1.00 17.82 A ATOM 1458 CBALA A 193 21.695 68.043 116.395 1.00 17.73 A ATOM 1459 C ALA A 19322.357 66.533 118.276 1.00 19.11 A ATOM 1460 O ALA A 193 22.269 66.978119.420 1.00 17.05 A ATOM 1461 N VAL A 194 22.033 65.279 117.973 1.0018.73 A ATOM 1462 CA VAL A 194 21.505 64.391 119.000 1.00 18.68 A ATOM1463 CB VAL A 194 20.586 63.299 118.366 1.00 20.01 A ATOM 1464 CG1 VAL A194 21.429 62.229 117.676 1.00 21.94 A ATOM 1465 CG2 VAL A 194 19.68162.688 119.427 1.00 20.08 A ATOM 1466 C VAL A 194 22.556 63.715 119.8941.00 18.19 A ATOM 1467 O VAL A 194 22.203 63.188 120.947 1.00 18.53 AATOM 1468 N THR A 195 23.830 63.737 119.497 1.00 18.59 A ATOM 1469 CATHR A 195 24.892 63.100 120.293 1.00 19.00 A ATOM 1470 CB THR A 19525.701 62.079 119.456 1.00 19.71 A ATOM 1471 OG1 THR A 195 26.401 62.754118.405 1.00 19.52 A ATOM 1472 CG2 THR A 195 24.785 61.028 118.860 1.0022.73 A ATOM 1473 C THR A 195 25.902 64.061 120.940 1.00 18.87 A ATOM1474 O THR A 195 26.621 63.692 121.870 1.00 18.50 A ATOM 1475 N PHE A196 25.971 65.290 120.454 1.00 19.16 A ATOM 1476 CA PHE A 196 26.91766.244 121.024 1.00 16.16 A ATOM 1477 CB PHE A 196 26.878 67.552 120.2301.00 17.37 A ATOM 1478 CG PHE A 196 27.756 68.625 120.797 1.00 18.14 AATOM 1479 CD1 PHE A 196 27.339 69.384 121.885 1.00 19.21 A ATOM 1480 CD2PHE A 196 29.030 68.834 120.285 1.00 17.83 A ATOM 1481 CE1 PHE A 19628.185 70.333 122.459 1.00 19.80 A ATOM 1482 CE2 PHE A 196 29.878 69.779120.854 1.00 18.39 A ATOM 1483 CZ PHE A 196 29.455 70.525 121.940 1.0016.80 A ATOM 1484 C PHE A 196 26.614 66.533 122.497 1.00 15.24 A ATOM1485 O PHE A 196 25.466 66.703 122.874 1.00 15.60 A ATOM 1486 N ARG A197 27.645 66.567 123.334 1.00 15.68 A ATOM 1487 CA ARG A 197 27.44766.885 124.745 1.00 17.09 A ATOM 1488 CB ARG A 197 26.765 65.729 125.5001.00 16.77 A ATOM 1489 CG ARG A 197 27.647 64.546 125.839 1.00 18.42 AATOM 1490 CD ARG A 197 26.830 63.452 126.527 1.00 17.90 A ATOM 1491 NEARG A 197 25.711 63.026 125.689 1.00 18.84 A ATOM 1492 CZ ARG A 19724.453 63.420 125.855 1.00 17.63 A ATOM 1493 NH1 ARG A 197 24.133 64.249126.843 1.00 16.56 A ATOM 1494 NH2 ARG A 197 23.517 63.008 125.012 1.0016.66 A ATOM 1495 C ARG A 197 28.758 67.250 125.421 1.00 17.09 A ATOM1496 O ARG A 197 29.842 66.951 124.904 1.00 16.37 A ATOM 1497 N GLY A198 28.642 67.909 126.572 1.00 16.23 A ATOM 1498 CA GLY A 198 29.80668.325 127.330 1.00 16.62 A ATOM 1499 C GLY A 198 30.669 67.174 127.8091.00 16.44 A ATOM 1500 O GLY A 198 30.266 66.010 127.727 1.00 17.18 AATOM 1501 N PRO A 199 31.866 67.470 128.330 1.00 16.69 A ATOM 1502 CDPRO A 199 32.552 68.775 128.239 1.00 16.86 A ATOM 1503 CA PRO A 19932.781 66.435 128.814 1.00 16.94 A ATOM 1504 CB PRO A 199 34.146 67.038128.518 1.00 17.97 A ATOM 1505 CG PRO A 199 33.912 68.487 128.865 1.0016.67 A ATOM 1506 C PRO A 199 32.643 66.060 130.280 1.00 18.52 A ATOM1507 O PRO A 199 32.167 66.841 131.097 1.00 17.68 A ATOM 1508 N SER A200 33.073 64.847 130.598 1.00 19.80 A ATOM 1509 CA SER A 200 33.05764.349 131.964 1.00 20.75 A ATOM 1510 CB SER A 200 31.718 63.701 132.3111.00 22.74 A ATOM 1511 OG SER A 200 31.780 63.121 133.608 1.00 23.95 AATOM 1512 C SER A 200 34.162 63.317 132.105 1.00 21.76 A ATOM 1513 O SERA 200 34.274 62.396 131.287 1.00 18.77 A ATOM 1514 N GLU A 201 34.97463.480 133.146 1.00 19.44 A ATOM 1515 CA GLU A 201 36.076 62.568 133.4251.00 22.42 A ATOM 1516 CB GLU A 201 36.836 63.045 134.670 1.00 23.51 AATOM 1517 CG GLU A 201 37.728 64.257 134.419 1.00 28.88 A ATOM 1518 CDGLU A 201 38.211 64.911 135.704 1.00 32.82 A ATOM 1519 OE1 GLU A 20138.427 64.177 136.694 1.00 32.22 A ATOM 1520 OE2 GLU A 201 38.381 66.156135.717 1.00 32.99 A ATOM 1521 C GLU A 201 35.554 61.152 133.646 1.0021.15 A ATOM 1522 O GLU A 201 36.291 60.176 133.492 1.00 21.69 A ATOM1523 N THR A 202 34.276 61.053 133.990 1.00 21.62 A ATOM 1524 CA THR A202 33.631 59.766 134.249 1.00 23.21 A ATOM 1525 CB THR A 202 32.43859.943 135.214 1.00 24.29 A ATOM 1526 OG1 THR A 202 31.389 60.665134.550 1.00 25.61 A ATOM 1527 CG2 THR A 202 32.870 60.724 136.454 1.0023.67 A ATOM 1528 C THR A 202 33.111 59.048 132.996 1.00 24.32 A ATOM1529 O THR A 202 32.641 57.909 133.087 1.00 23.55 A ATOM 1530 N ASP A203 33.206 59.699 131.837 1.00 24.26 A ATOM 1531 CA ASP A 203 32.70659.123 130.586 1.00 23.45 A ATOM 1532 CB ASP A 203 31.356 59.772 130.2531.00 23.20 A ATOM 1533 CG ASP A 203 30.514 58.945 129.295 1.00 24.79 AATOM 1534 OD1 ASP A 203 29.302 59.243 129.174 1.00 25.03 A ATOM 1535 OD2ASP A 203 31.045 58.010 128.664 1.00 23.91 A ATOM 1536 C ASP A 20333.691 59.328 129.430 1.00 23.07 A ATOM 1537 O ASP A 203 33.483 60.191128.572 1.00 20.44 A ATOM 1538 N MET A 204 34.761 58.535 129.410 1.0021.83 A ATOM 1539 CA MET A 204 35.771 58.643 128.362 1.00 21.76 A ATOM1540 CB MET A 204 37.010 57.808 128.720 1.00 24.97 A ATOM 1541 CG MET A204 37.825 58.362 129.886 1.00 27.70 A ATOM 1542 SD MET A 204 38.36060.089 129.663 1.00 29.97 A ATOM 1543 CE MET A 204 37.140 60.917 130.5711.00 29.70 A ATOM 1544 C MET A 204 35.225 58.200 127.010 1.00 22.24 AATOM 1545 O MET A 204 35.629 58.722 125.967 1.00 20.89 A ATOM 1546 N ASPA 205 34.309 57.232 127.032 1.00 21.97 A ATOM 1547 CA ASP A 205 33.69056.736 125.805 1.00 22.89 A ATOM 1548 CB ASP A 205 32.629 55.690 126.1331.00 25.54 A ATOM 1549 CG ASP A 205 33.214 54.327 126.373 1.00 29.64 AATOM 1550 OD1 ASP A 205 34.441 54.243 126.610 1.00 29.17 A ATOM 1551 OD2ASP A 205 32.441 53.343 126.332 1.00 27.49 A ATOM 1552 C ASP A 20533.023 57.883 125.071 1.00 21.88 A ATOM 1553 O ASP A 205 33.260 58.105123.884 1.00 19.23 A ATOM 1554 N SER A 206 32.172 58.606 125.793 1.0021.39 A ATOM 1555 CA SER A 206 31.452 59.726 125.210 1.00 22.34 A ATOM1556 CB SER A 206 30.534 60.361 126.260 1.00 24.35 A ATOM 1557 OG SER A206 29.801 61.441 125.711 1.00 28.36 A ATOM 1558 C SER A 206 32.41960.765 124.651 1.00 22.11 A ATOM 1559 O SER A 206 32.205 61.294 123.5601.00 22.41 A ATOM 1560 N LEU A 207 33.489 61.042 125.395 1.00 20.55 AATOM 1561 CA LEU A 207 34.487 62.018 124.972 1.00 19.96 A ATOM 1562 CBLEU A 207 35.563 62.184 126.055 1.00 19.69 A ATOM 1563 CG LEU A 20736.586 63.301 125.825 1.00 21.16 A ATOM 1564 CD1 LEU A 207 35.909 64.664125.936 1.00 20.91 A ATOM 1565 CD2 LEU A 207 37.712 63.182 126.845 1.0022.85 A ATOM 1566 C LEU A 207 35.129 61.598 123.648 1.00 18.93 A ATOM1567 O LEU A 207 35.369 62.430 122.778 1.00 19.49 A ATOM 1568 N VAL A208 35.402 60.304 123.491 1.00 19.50 A ATOM 1569 CA VAL A 208 35.99359.811 122.252 1.00 18.09 A ATOM 1570 CB VAL A 208 36.308 58.299 122.3511.00 19.75 A ATOM 1571 CG1 VAL A 208 36.723 57.760 120.995 1.00 22.42 AATOM 1572 CG2 VAL A 208 37.408 58.068 123.378 1.00 22.62 A ATOM 1573 CVAL A 208 35.020 60.059 121.090 1.00 18.11 A ATOM 1574 O VAL A 20835.428 60.418 119.982 1.00 17.15 A ATOM 1575 N GLY A 209 33.730 59.875121.349 1.00 17.76 A ATOM 1576 CA GLY A 209 32.744 60.102 120.308 1.0018.19 A ATOM 1577 C GLY A 209 32.715 61.554 119.858 1.00 19.02 A ATOM1578 O GLY A 209 32.445 61.843 118.689 1.00 20.34 A ATOM 1579 N GLN A210 32.993 62.472 120.780 1.00 17.40 A ATOM 1580 CA GLN A 210 32.98763.901 120.465 1.00 17.84 A ATOM 1581 CB GLN A 210 33.053 64.729 121.7541.00 16.99 A ATOM 1582 CG GLN A 210 31.942 64.396 122.742 1.00 19.21 AATOM 1583 CD GLN A 210 30.542 64.568 122.154 1.00 20.53 A ATOM 1584 OE1GLN A 210 29.627 63.805 122.470 1.00 20.22 A ATOM 1585 NE2 GLN A 21030.369 65.578 121.314 1.00 12.91 A ATOM 1586 C GLN A 210 34.133 64.284119.534 1.00 16.80 A ATOM 1587 O GLN A 210 34.113 65.350 118.921 1.0018.59 A ATOM 1588 N ALA A 211 35.123 63.405 119.415 1.00 16.27 A ATOM1589 CA ALA A 211 36.268 63.654 118.546 1.00 16.35 A ATOM 1590 CB ALA A211 37.552 63.197 119.239 1.00 18.22 A ATOM 1591 C ALA A 211 36.11562.931 117.207 1.00 15.81 A ATOM 1592 O ALA A 211 36.803 63.251 116.2271.00 16.08 A ATOM 1593 N LEU A 212 35.192 61.976 117.166 1.00 14.42 AATOM 1594 CA LEU A 212 34.961 61.172 115.968 1.00 15.87 A ATOM 1595 CBLEU A 212 34.778 59.703 116.370 1.00 15.09 A ATOM 1596 CG LEU A 21235.978 58.937 116.915 1.00 20.51 A ATOM 1597 CD1 LEU A 212 35.522 57.536117.328 1.00 20.17 A ATOM 1598 CD2 LEU A 212 37.067 58.856 115.853 1.0020.66 A ATOM 1599 C LEU A 212 33.805 61.529 115.040 1.00 15.76 A ATOM1600 O LEU A 212 33.991 61.646 113.830 1.00 17.03 A ATOM 1601 N PHE A213 32.609 61.675 115.605 1.00 16.08 A ATOM 1602 CA PHE A 213 31.40861.918 114.806 1.00 16.97 A ATOM 1603 CB PHE A 213 30.164 61.636 115.6511.00 17.71 A ATOM 1604 CG PHE A 213 30.186 60.292 116.314 1.00 20.56 AATOM 1605 CD1 PHE A 213 30.512 59.152 115.587 1.00 22.69 A ATOM 1606 CD2PHE A 213 29.923 60.168 117.671 1.00 21.84 A ATOM 1607 CE1 PHE A 21330.583 57.913 116.206 1.00 24.50 A ATOM 1608 CE2 PHE A 213 29.992 58.928118.297 1.00 22.58 A ATOM 1609 CZ PHE A 213 30.323 57.805 117.566 1.0020.73 A ATOM 1610 C PHE A 213 31.260 63.254 114.101 1.00 15.36 A ATOM1611 O PHE A 213 31.551 64.304 114.659 1.00 12.76 A ATOM 1612 N ALA A214 30.771 63.184 112.863 1.00 16.63 A ATOM 1613 CA ALA A 214 30.58664.363 112.018 1.00 15.40 A ATOM 1614 CB ALA A 214 31.759 64.497 111.0501.00 16.43 A ATOM 1615 C ALA A 214 29.276 64.260 111.243 1.00 15.29 AATOM 1616 O ALA A 214 28.595 63.232 111.301 1.00 16.79 A ATOM 1617 N ASPA 215 28.946 65.316 110.502 1.00 16.01 A ATOM 1618 CA ASP A 215 27.70065.379 109.735 1.00 15.93 A ATOM 1619 CB ASP A 215 26.972 66.703 109.9981.00 17.66 A ATOM 1620 CG ASP A 215 26.788 66.996 111.474 1.00 22.88 AATOM 1621 OD1 ASP A 215 26.964 66.080 112.302 1.00 22.93 A ATOM 1622 OD2ASP A 215 26.452 68.151 111.805 1.00 21.11 A ATOM 1623 C ASP A 21527.896 65.251 108.231 1.00 13.47 A ATOM 1624 O ASP A 215 28.892 65.710107.682 1.00 12.91 A ATOM 1625 N GLY A 216 26.914 64.642 107.571 1.0014.99 A ATOM 1626 CA GLY A 216 26.969 64.472 106.135 1.00 14.98 A ATOM1627 C GLY A 216 25.807 63.636 105.626 1.00 15.88 A ATOM 1628 O GLY A216 25.154 62.929 106.398 1.00 14.93 A ATOM 1629 N ALA A 217 25.53763.731 104.329 1.00 16.39 A ATOM 1630 CA ALA A 217 24.461 62.961 103.7191.00 15.08 A ATOM 1631 CB ALA A 217 23.207 63.820 103.543 1.00 14.14 AATOM 1632 C ALA A 217 24.925 62.454 102.373 1.00 14.86 A ATOM 1633 O ALAA 217 25.679 63.121 101.666 1.00 15.64 A ATOM 1634 N ALA A 218 24.47861.256 102.027 1.00 13.54 A ATOM 1635 CA ALA A 218 24.828 60.671 100.7501.00 14.40 A ATOM 1636 CB ALA A 218 25.784 59.499 100.950 1.00 13.37 AATOM 1637 C ALA A 218 23.521 60.202 100.131 1.00 14.12 A ATOM 1638 O ALAA 218 22.622 59.752 100.845 1.00 15.69 A ATOM 1639 N ALA A 219 23.40860.336 98.815 1.00 14.03 A ATOM 1640 CA ALA A 219 22.212 59.908 98.1031.00 15.39 A ATOM 1641 CB ALA A 219 21.447 61.112 97.556 1.00 15.27 AATOM 1642 C ALA A 219 22.667 59.003 96.971 1.00 14.28 A ATOM 1643 O ALAA 219 23.623 59.315 96.251 1.00 14.99 A ATOM 1644 N ILE A 220 21.97457.882 96.823 1.00 13.67 A ATOM 1645 CA ILE A 220 22.325 56.893 95.8191.00 13.44 A ATOM 1646 CB ILE A 220 22.991 55.672 96.495 1.00 14.33 AATOM 1647 CG2 ILE A 220 23.609 54.782 95.461 1.00 14.98 A ATOM 1648 CG1ILE A 220 24.037 56.134 97.515 1.00 14.70 A ATOM 1649 CD1 ILE A 22023.478 56.354 98.914 1.00 16.90 A ATOM 1650 C ILE A 220 21.114 56.38995.029 1.00 13.38 A ATOM 1651 O ILE A 220 20.061 56.123 95.598 1.0014.24 A ATOM 1652 N ILE A 221 21.273 56.264 93.717 1.00 13.12 A ATOM1653 CA ILE A 221 20.207 55.747 92.867 1.00 14.15 A ATOM 1654 CB ILE A221 20.057 56.561 91.562 1.00 15.24 A ATOM 1655 CG2 ILE A 221 18.98455.924 90.679 1.00 14.91 A ATOM 1656 CG1 ILE A 221 19.692 58.013 91.8861.00 16.31 A ATOM 1657 CD1 ILE A 221 18.300 58.187 92.471 1.00 17.99 AATOM 1658 C ILE A 221 20.623 54.331 92.496 1.00 15.28 A ATOM 1659 O ILEA 221 21.730 54.121 91.989 1.00 14.96 A ATOM 1660 N ILE A 222 19.73553.372 92.749 1.00 15.38 A ATOM 1661 CA ILE A 222 19.995 51.971 92.4431.00 15.44 A ATOM 1662 CB ILE A 222 20.102 51.136 93.720 1.00 16.28 AATOM 1663 CG2 ILE A 222 20.159 49.646 93.368 1.00 15.57 A ATOM 1664 CG1ILE A 222 21.346 51.553 94.510 1.00 21.06 A ATOM 1665 CD1 ILE A 22221.400 50.945 95.884 1.00 23.56 A ATOM 1666 C ILE A 222 18.881 51.36591.595 1.00 15.66 A ATOM 1667 O ILE A 222 17.703 51.641 91.818 1.0012.27 A ATOM 1668 N GLY A 223 19.263 50.531 90.634 1.00 13.58 A ATOM1669 CA GLY A 223 18.270 49.885 89.792 1.00 15.55 A ATOM 1670 C GLY A223 18.839 48.726 88.998 1.00 15.80 A ATOM 1671 O GLY A 223 20.04048.677 88.737 1.00 15.51 A ATOM 1672 N SER A 224 17.985 47.777 88.6301.00 15.62 A ATOM 1673 CA SER A 224 18.426 46.645 87.819 1.00 17.60 AATOM 1674 CB SER A 224 17.697 45.357 88.235 1.00 17.65 A ATOM 1675 CGSER A 224 18.151 44.877 89.495 1.00 15.67 A ATOM 1676 C SER A 224 18.10646.970 86.352 1.00 18.97 A ATOM 1677 O SER A 224 17.281 47.835 86.0741.00 16.29 A ATOM 1678 N ASP A 225 18.772 46.288 85.427 1.00 19.29 AATOM 1679 CA ASP A 225 18.550 46.486 83.996 1.00 20.50 A ATOM 1680 CBASP A 225 17.159 45.973 83.610 1.00 22.70 A ATOM 1681 CG ASP A 22516.916 44.546 84.075 1.00 24.43 A ATOM 1682 OD1 ASP A 225 17.893 43.77384.138 1.00 25.70 A ATOM 1683 OD2 ASP A 225 15.752 44.198 84.366 1.0025.65 A ATOM 1684 C ASP A 225 18.695 47.941 83.559 1.00 21.75 A ATOM1685 O ASP A 225 17.724 48.571 83.124 1.00 19.34 A ATOM 1686 N PRO A 22619.910 48.499 83.675 1.00 22.11 A ATOM 1687 CD PRO A 226 21.149 47.91584.216 1.00 22.58 A ATOM 1688 CA PRO A 226 20.113 49.893 83.272 1.0022.76 A ATOM 1689 CB PRO A 226 21.543 50.183 83.726 1.00 23.77 A ATOM1690 CG PRO A 226 22.201 48.835 83.655 1.00 24.27 A ATOM 1691 C PRO A226 19.917 50.108 81.776 1.00 24.18 A ATOM 1692 O PRO A 226 20.35949.300 80.959 1.00 23.57 A ATOM 1693 N VAL A 227 19.241 51.200 81.4331.00 25.11 A ATOM 1694 CA VAL A 227 18.983 51.552 80.041 1.00 27.09 AATOM 1695 CB VAL A 227 18.034 52.766 79.941 1.00 27.14 A ATOM 1696 CG1VAL A 227 17.822 53.145 78.475 1.00 28.54 A ATOM 1697 CG2 VAL A 22716.704 52.444 80.614 1.00 26.13 A ATOM 1698 C VAL A 227 20.309 51.90979.385 1.00 29.32 A ATOM 1699 O VAL A 227 20.960 52.883 79.762 1.0030.05 A ATOM 1700 N PRO A 228 20.726 51.127 78.382 1.00 31.26 A ATOM1701 CD PRO A 228 19.997 50.035 77.714 1.00 31.51 A ATOM 1702 CA PRO A228 21.994 51.402 77.707 1.00 32.21 A ATOM 1703 CB PRO A 228 22.09750.258 76.698 1.00 33.57 A ATOM 1704 CG PRO A 228 20.662 49.991 76.3581.00 33.69 A ATOM 1705 C PRO A 228 22.077 52.779 77.053 1.00 33.32 AATOM 1706 O PRO A 228 21.109 53.270 76.468 1.00 33.41 A ATOM 1707 N GLUA 229 23.245 53.398 77.180 1.00 35.15 A ATOM 1708 CA GLU A 229 23.51054.708 76.600 1.00 35.98 A ATOM 1709 CB GLU A 229 23.274 54.662 75.0861.00 39.82 A ATOM 1710 CG GLU A 229 24.112 55.656 74.289 1.00 44.78 AATOM 1711 CD GLU A 229 25.586 55.274 74.233 1.00 48.37 A ATOM 1712 OE1GLU A 229 26.221 55.162 75.307 1.00 50.63 A ATOM 1713 OE2 GLU A 22926.111 55.087 73.113 1.00 49.28 A ATOM 1714 C GLU A 229 22.677 55.83077.221 1.00 34.20 A ATOM 1715 O GLU A 229 22.714 56.969 76.751 1.0034.48 A ATOM 1716 N VAL A 230 21.926 55.509 78.270 1.00 30.04 A ATOM1717 CA VAL A 230 21.109 56.508 78.956 1.00 27.19 A ATOM 1718 CB VAL A230 19.614 56.160 78.878 1.00 28.09 A ATOM 1719 CG1 VAL A 230 18.81057.139 79.712 1.00 26.44 A ATOM 1720 CG2 VAL A 230 19.153 56.198 77.4281.00 29.81 A ATOM 1721 C VAL A 230 21.543 56.580 80.418 1.00 25.17 AATOM 1722 O VAL A 230 21.904 57.643 80.919 1.00 24.16 A ATOM 1723 N GLUA 231 21.498 55.442 81.099 1.00 20.97 A ATOM 1724 CA GLU A 231 21.92955.371 82.491 1.00 22.09 A ATOM 1725 CB GLU A 231 21.017 54.425 83.2851.00 19.51 A ATOM 1726 CG GLU A 231 19.598 54.962 83.442 1.00 20.55 AATOM 1727 CD GLU A 231 18.638 53.974 84.084 1.00 18.71 A ATOM 1728 OE1GLU A 231 18.623 52.804 83.655 1.00 19.07 A ATOM 1729 OE2 GLU A 23117.890 54.370 85.004 1.00 17.90 A ATOM 1730 C GLU A 231 23.367 54.85582.460 1.00 22.54 A ATOM 1731 O GLU A 231 23.778 54.217 81.487 1.0023.20 A ATOM 1732 N LYS A 232 24.136 55.120 83.511 1.00 22.05 A ATOM1733 CA LYS A 232 25.525 54.684 83.522 1.00 22.17 A ATOM 1734 CB LYS A232 26.435 55.886 83.249 1.00 25.60 A ATOM 1735 CG LYS A 232 26.10656.608 81.942 1.00 30.76 A ATOM 1736 CD LYS A 232 26.256 55.672 80.7451.00 36.23 A ATOM 1737 CE LYS A 232 25.664 56.271 79.471 1.00 38.29 AATOM 1738 NZ LYS A 232 26.334 57.539 79.069 1.00 37.95 A ATOM 1739 C LYSA 232 25.956 53.989 84.807 1.00 21.43 A ATOM 1740 O LYS A 232 26.19154.635 85.831 1.00 18.89 A ATOM 1741 N PRO A 233 26.076 52.653 84.7621.00 20.17 A ATOM 1742 CD PRO A 233 25.704 51.783 83.629 1.00 19.69 AATOM 1743 CA PRO A 233 26.485 51.853 85.920 1.00 18.06 A ATOM 1744 CBPRO A 233 26.556 50.441 85.348 1.00 17.95 A ATOM 1745 CG PRO A 23325.475 50.451 84.307 1.00 19.68 A ATOM 1746 C PRO A 233 27.820 52.29786.523 1.00 17.74 A ATOM 1747 O PRO A 233 28.701 52.797 85.814 1.0017.95 A ATOM 1748 N ILE A 234 27.955 52.107 87.833 1.00 16.92 A ATOM1749 CA ILE A 234 29.174 52.449 88.566 1.00 16.46 A ATOM 1750 CB ILE A234 28.901 53.555 89.610 1.00 17.04 A ATOM 1751 CG2 ILE A 234 30.20453.975 90.274 1.00 17.44 A ATOM 1752 CG1 ILE A 234 28.248 54.759 88.9261.00 16.08 A ATOM 1753 CD1 ILE A 234 27.885 55.908 89.868 1.00 15.92 AATOM 1754 C ILE A 234 29.695 51.194 89.282 1.00 16.04 A ATOM 1755 O ILEA 234 30.876 50.859 89.191 1.00 15.88 A ATOM 1756 N PHE A 235 28.79950.509 89.987 1.00 14.55 A ATOM 1757 CA PHE A 235 29.125 49.275 90.7031.00 15.26 A ATOM 1758 CB PHE A 235 29.483 49.545 92.174 1.00 15.43 AATOM 1759 CG PHE A 235 30.769 50.301 92.372 1.00 16.25 A ATOM 1760 CD1PHE A 235 31.996 49.687 92.154 1.00 15.90 A ATOM 1761 CD2 PHE A 23530.745 51.633 92.788 1.00 17.19 A ATOM 1762 CE1 PHE A 235 33.194 50.38692.346 1.00 17.25 A ATOM 1763 CE2 PHE A 235 31.927 52.344 92.983 1.0014.62 A ATOM 1764 CZ PHE A 235 33.157 51.723 92.762 1.00 15.37 A ATOM1765 C PHE A 235 27.870 48.414 90.681 1.00 16.08 A ATOM 1766 O PHE A 23526.763 48.938 90.602 1.00 15.87 A ATOM 1767 N GLU A 236 28.043 47.09990.739 1.00 15.93 A ATOM 1768 CA GLU A 236 26.907 46.180 90.781 1.0016.34 A ATOM 1769 CB GLU A 236 27.027 45.090 89.715 1.00 17.35 A ATOM1770 CG GLU A 236 27.058 45.559 88.281 1.00 20.47 A ATOM 1771 CD GLU A236 26.908 44.398 87.313 1.00 25.69 A ATOM 1772 OE1 GLU A 236 27.46043.312 87.600 1.00 24.01 A ATOM 1773 OE2 GLU A 236 26.248 44.571 86.2671.00 28.51 A ATOM 1774 C GLU A 236 26.949 45.504 92.149 1.00 16.24 AATOM 1775 O GLU A 236 28.034 45.240 92.673 1.00 17.59 A ATOM 1776 N LEUA 237 25.781 45.226 92.721 1.00 16.37 A ATOM 1777 CA LEU A 237 25.69544.558 94.013 1.00 17.59 A ATOM 1778 CB LEU A 237 24.447 45.034 94.7641.00 18.64 A ATOM 1779 CG LEU A 237 24.363 46.549 95.008 1.00 18.69 AATOM 1780 CD1 LEU A 237 23.085 46.887 95.785 1.00 18.52 A ATOM 1781 CD2LEU A 237 25.589 47.006 95.779 1.00 19.96 A ATOM 1782 C LEU A 237 25.62943.050 93.746 1.00 18.31 A ATOM 1783 O LEU A 237 24.752 42.586 93.0251.00 18.78 A ATOM 1784 N VAL A 238 26.557 42.297 94.329 1.00 19.02 AATOM 1785 CA VAL A 238 26.637 40.849 94.127 1.00 18.34 A ATOM 1786 CBVAL A 238 28.117 40.419 93.976 1.00 19.89 A ATOM 1787 CG1 VAL A 23828.216 38.929 93.689 1.00 20.10 A ATOM 1788 CG2 VAL A 238 28.765 41.21392.855 1.00 19.49 A ATOM 1789 C VAL A 238 25.982 40.027 95.243 1.0018.89 A ATOM 1790 O VAL A 238 25.114 39.187 94.989 1.00 18.23 A ATOM1791 N SER A 239 26.410 40.259 96.479 1.00 17.69 A ATOM 1792 CA SER A239 25.853 39.544 97.621 1.00 18.25 A ATOM 1793 CB SER A 239 26.62638.252 97.890 1.00 18.69 A ATOM 1794 OG SER A 239 27.964 38.546 98.2281.00 19.05 A ATOM 1795 C SER A 239 25.935 40.437 98.844 1.00 18.67 AATOM 1796 O SER A 239 26.749 41.352 98.892 1.00 18.20 A ATOM 1797 N THRA 240 25.079 40.167 99.823 1.00 20.47 A ATOM 1798 CA THR A 240 25.04040.933 101.061 1.00 21.73 A ATOM 1799 CB THR A 240 23.894 41.977 101.0381.00 22.77 A ATOM 1800 OG1 THR A 240 22.642 41.316 100.814 1.00 23.88 AATOM 1801 CG2 THR A 240 24.115 42.997 99.928 1.00 23.12 A ATOM 1802 CTHR A 240 24.819 39.988 102.241 1.00 22.20 A ATOM 1803 O THR A 24023.843 39.236 102.264 1.00 23.37 A ATOM 1804 N ASP A 241 25.738 40.011103.203 1.00 19.70 A ATOM 1805 CA ASP A 241 25.636 39.175 104.397 1.0018.27 A ATOM 1806 CB ASP A 241 26.845 38.232 104.520 1.00 20.13 A ATOM1807 CG ASP A 241 26.980 37.278 103.344 1.00 21.50 A ATOM 1808 OD1 ASP A241 25.994 36.577 103.024 1.00 21.04 A ATOM 1809 OD2 ASP A 241 28.08237.220 102.746 1.00 20.42 A ATOM 1810 C ASP A 241 25.622 40.096 105.6161.00 18.38 A ATOM 1811 O ASP A 241 26.094 41.234 105.545 1.00 17.12 AATOM 1812 N GLN A 242 25.063 39.613 106.722 1.00 14.47 A ATOM 1813 CAGLN A 242 25.039 40.379 107.961 1.00 17.92 A ATOM 1814 CB GLN A 24223.684 41.068 108.189 1.00 16.66 A ATOM 1815 CG GLN A 242 23.701 42.010109.410 1.00 18.83 A ATOM 1816 CD GLN A 242 22.334 42.557 109.787 1.0017.48 A ATOM 1817 OE1 GLN A 242 21.344 41.834 109.772 1.00 21.26 A ATOM1818 NE2 GLN A 242 22.281 43.837 110.162 1.00 17.14 A ATOM 1819 C GLN A242 25.309 39.389 109.083 1.00 17.83 A ATOM 1820 O GLN A 242 24.85838.244 109.023 1.00 19.34 A ATOM 1821 N LYS A 243 26.047 39.817 110.0991.00 18.25 A ATOM 1822 CA LYS A 243 26.354 38.927 111.209 1.00 17.86 AATOM 1823 CB LYS A 243 27.610 38.114 110.910 1.00 18.91 A ATOM 1824 CGLYS A 243 27.935 37.098 112.007 1.00 20.00 A ATOM 1825 CD LYS A 24329.136 36.244 111.667 1.00 22.37 A ATOM 1826 CE LYS A 243 29.250 35.069112.631 1.00 26.37 A ATOM 1827 NZ LYS A 243 29.364 35.524 114.037 1.0025.10 A ATOM 1828 C LYS A 243 26.552 39.623 112.548 1.00 19.29 A ATOM1829 O LYS A 243 27.176 40.687 112.633 1.00 16.88 A ATOM 1830 N LEU A244 26.019 38.993 113.589 1.00 18.07 A ATOM 1831 CA LEU A 244 26.15139.481 114.950 1.00 18.71 A ATOM 1832 CB LEU A 244 24.867 39.232 115.7461.00 19.92 A ATOM 1833 CG LEU A 244 23.763 40.289 115.745 1.00 21.98 AATOM 1834 CD1 LEU A 244 22.516 39.719 116.407 1.00 21.24 A ATOM 1835 CD2LEU A 244 24.248 41.533 116.491 1.00 22.15 A ATOM 1836 C LEU A 24427.272 38.675 115.582 1.00 18.89 A ATOM 1837 O LEU A 244 27.307 37.453115.456 1.00 18.50 A ATOM 1838 N VAL A 245 28.200 39.354 116.241 1.0019.19 A ATOM 1839 CA VAL A 245 29.286 38.656 116.919 1.00 20.00 A ATOM1840 CB VAL A 245 30.556 39.522 116.976 1.00 21.57 A ATOM 1841 CG1 VAL A245 31.655 38.800 117.743 1.00 19.12 A ATOM 1842 CG2 VAL A 245 31.01739.838 115.553 1.00 22.63 A ATOM 1843 C VAL A 245 28.783 38.368 118.3321.00 19.85 A ATOM 1844 O VAL A 245 28.518 39.288 119.114 1.00 17.71 AATOM 1845 N PRO A 246 28.623 37.081 118.672 1.00 19.89 A ATOM 1846 CDPRO A 246 28.880 35.885 117.856 1.00 21.03 A ATOM 1847 CA PRO A 24628.142 36.706 120.006 1.00 21.13 A ATOM 1848 CB PRO A 246 28.244 35.182119.996 1.00 21.02 A ATOM 1849 CG PRO A 246 28.038 34.840 118.561 1.0021.01 A ATOM 1850 C PRO A 246 28.978 37.320 121.117 1.00 19.52 A ATOM1851 O PRO A 246 30.173 37.545 120.950 1.00 20.14 A ATOM 1852 N GLY A247 28.329 37.593 122.243 1.00 21.22 A ATOM 1853 CA GLY A 247 29.00638.152 123.399 1.00 21.01 A ATOM 1854 C GLY A 247 29.635 39.525 123.2421.00 22.29 A ATOM 1855 O GLY A 247 30.659 39.802 123.863 1.00 23.76 AATOM 1856 N SER A 248 29.034 40.396 122.439 1.00 20.11 A ATOM 1857 CASER A 248 29.607 41.724 122.257 1.00 19.92 A ATOM 1858 CB SER A 24830.412 41.774 120.952 1.00 19.95 A ATOM 1859 OG SER A 248 29.602 41.489119.822 1.00 20.22 A ATOM 1860 C SER A 248 28.584 42.854 122.282 1.0019.40 A ATOM 1861 O SER A 248 28.761 43.870 121.613 1.00 18.71 A ATOM1862 N HIS A 249 27.524 42.692 123.068 1.00 19.08 A ATOM 1863 CA HIS A249 26.494 43.729 123.156 1.00 20.12 A ATOM 1864 CB HIS A 249 25.36443.277 124.088 1.00 21.72 A ATOM 1865 CG HIS A 249 24.341 44.339 124.3591.00 21.96 A ATOM 1866 CD2 HIS A 249 24.221 45.219 125.382 1.00 23.31 AATOM 1867 ND1 HIS A 249 23.290 44.600 123.505 1.00 24.75 A ATOM 1868 CE1HIS A 249 22.566 45.593 123.991 1.00 20.55 A ATOM 1869 NE2 HIS A 24923.110 45.988 125.128 1.00 23.96 A ATOM 1870 C HIS A 249 27.087 45.037123.682 1.00 20.12 A ATOM 1871 O HIS A 249 26.687 46.133 123.261 1.0017.34 A ATOM 1872 N GLY A 250 28.045 44.908 124.599 1.00 18.18 A ATOM1873 CA GLY A 250 28.679 46.074 125.196 1.00 21.10 A ATOM 1874 C GLY A250 29.815 46.741 124.427 1.00 21.47 A ATOM 1875 O GLY A 250 30.43947.677 124.938 1.00 21.77 A ATOM 1876 N ALA A 251 30.087 46.286 123.2061.00 19.97 A ATOM 1877 CA ALA A 251 31.160 46.869 122.407 1.00 20.87 AATOM 1878 CB ALA A 251 31.528 45.932 121.257 1.00 21.00 A ATOM 1879 CALA A 251 30.785 48.252 121.858 1.00 21.86 A ATOM 1880 O ALA A 25131.551 49.209 121.990 1.00 20.74 A ATOM 1881 N ILE A 252 29.611 48.350121.242 1.00 20.93 A ATOM 1882 CA ILE A 252 29.147 49.615 120.667 1.0022.07 A ATOM 1883 CB ILE A 252 29.434 49.698 119.155 1.00 24.82 A ATOM1884 CG2 ILE A 252 29.122 51.102 118.649 1.00 25.36 A ATOM 1885 CG1 ILEA 252 30.889 49.343 118.861 1.00 26.65 A ATOM 1886 CD1 ILE A 252 31.15449.143 117.378 1.00 29.75 A ATOM 1887 C ILE A 252 27.636 49.709 120.8141.00 20.47 A ATOM 1888 O ILE A 252 26.922 48.788 120.440 1.00 19.94 AATOM 1889 N GLY A 253 27.143 50.826 121.336 1.00 18.99 A ATOM 1890 CAGLY A 253 25.709 50.958 121.488 1.00 18.83 A ATOM 1891 C GLY A 25325.288 52.292 122.059 1.00 18.02 A ATOM 1892 O GLY A 253 26.093 53.220122.166 1.00 16.78 A ATOM 1893 N GLY A 254 24.019 52.378 122.429 1.0018.04 A ATOM 1894 CA GLY A 254 23.503 53.610 122.981 1.00 19.32 A ATOM1895 C GLY A 254 22.028 53.515 123.295 1.00 19.30 A ATOM 1896 O GLY A254 21.379 52.497 123.029 1.00 18.05 A ATOM 1897 N LEU A 255 21.51054.587 123.885 1.00 18.15 A ATOM 1898 CA LEU A 255 20.107 54.686 124.2511.00 17.89 A ATOM 1899 CB LEU A 255 19.909 54.384 125.734 1.00 19.68 AATOM 1900 CG LEU A 255 20.124 52.976 126.283 1.00 23.45 A ATOM 1901 CD1LEU A 255 19.989 53.011 127.798 1.00 23.78 A ATOM 1902 CD2 LEU A 25519.114 52.020 125.679 1.00 23.72 A ATOM 1903 C LEU A 255 19.653 56.112124.006 1.00 18.61 A ATOM 1904 O LEU A 255 20.425 57.053 124.198 1.0018.26 A ATOM 1905 N LEU A 256 18.408 56.275 123.575 1.00 17.55 A ATOM1906 CA LEU A 256 17.871 57.608 123.367 1.00 17.89 A ATOM 1907 CB LEU A256 16.779 57.596 122.291 1.00 17.89 A ATOM 1908 CG LEU A 256 16.20158.956 121.868 1.00 19.06 A ATOM 1909 CD1 LEU A 256 17.325 59.921121.508 1.00 19.37 A ATOM 1910 CD2 LEU A 256 15.260 58.763 120.680 1.0017.30 A ATOM 1911 C LEU A 256 17.297 57.972 124.733 1.00 17.61 A ATOM1912 O LEU A 256 16.453 57.262 125.276 1.00 17.82 A ATOM 1913 N ARG A257 17.765 59.076 125.296 1.00 17.36 A ATOM 1914 CA ARG A 257 17.31959.491 126.617 1.00 16.80 A ATOM 1915 CB ARG A 257 18.474 59.343 127.6091.00 17.15 A ATOM 1916 CG ARG A 257 19.105 57.958 127.670 1.00 18.55 AATOM 1917 CD ARG A 257 18.355 57.031 128.616 1.00 17.31 A ATOM 1918 NEARG A 257 17.311 56.261 127.945 1.00 17.17 A ATOM 1919 CZ ARG A 25716.626 55.279 128.525 1.00 16.27 A ATOM 1920 NH1 ARG A 257 16.871 54.952129.790 1.00 13.61 A ATOM 1921 NH2 ARG A 257 15.722 54.600 127.833 1.0016.69 A ATOM 1922 C ARG A 257 16.852 60.940 126.624 1.00 17.15 A ATOM1923 O ARG A 257 16.933 61.637 125.612 1.00 16.73 A ATOM 1924 N GLU A258 16.381 61.390 127.782 1.00 17.18 A ATOM 1925 CA GLU A 258 15.91362.757 127.926 1.00 17.36 A ATOM 1926 CB GLU A 258 15.210 62.911 129.2831.00 20.05 A ATOM 1927 CG GLU A 258 14.011 61.956 129.408 1.00 22.85 AATOM 1928 CD GLU A 258 13.427 61.842 130.811 1.00 25.37 A ATOM 1929 OE1GLU A 258 12.878 60.761 131.128 1.00 19.60 A ATOM 1930 OE2 GLU A 25813.497 62.819 131.590 1.00 24.69 A ATOM 1931 C GLU A 258 17.074 63.743127.755 1.00 16.92 A ATOM 1932 O GLU A 258 16.857 64.935 127.509 1.0017.03 A ATOM 1933 N VAL A 259 18.304 63.238 127.858 1.00 16.14 A ATOM1934 CA VAL A 259 19.492 64.066 127.679 1.00 16.37 A ATOM 1935 CB VAL A259 20.598 63.720 128.707 1.00 16.27 A ATOM 1936 CG1 VAL A 259 20.03563.814 130.117 1.00 18.16 A ATOM 1937 CG2 VAL A 259 21.158 62.319128.428 1.00 18.20 A ATOM 1938 C VAL A 259 20.072 63.891 126.276 1.0015.70 A ATOM 1939 O VAL A 259 21.175 64.360 125.984 1.00 13.21 A ATOM1940 N GLY A 260 19.323 63.210 125.411 1.00 17.11 A ATOM 1941 CA GLY A260 19.779 62.983 124.052 1.00 16.11 A ATOM 1942 C GLY A 260 20.21861.545 123.847 1.00 16.55 A ATOM 1943 O GLY A 260 19.886 60.674 124.6441.00 17.86 A ATOM 1944 N LEU A 261 20.968 61.294 122.781 1.00 15.96 AATOM 1945 CA LEU A 261 21.442 59.946 122.485 1.00 18.55 A ATOM 1946 CBLEU A 261 21.558 59.750 120.967 1.00 20.11 A ATOM 1947 CG LEU A 26122.175 58.437 120.472 1.00 20.59 A ATOM 1948 CD1 LEU A 261 21.420 57.265121.058 1.00 21.27 A ATOM 1949 CD2 LEU A 261 22.126 58.391 118.943 1.0021.87 A ATOM 1950 C LEU A 261 22.794 59.680 123.143 1.00 19.66 A ATOM1951 O LEU A 261 23.817 60.224 122.730 1.00 21.17 A ATOM 1952 N THR A262 22.788 58.852 124.176 1.00 19.32 A ATOM 1953 CA THR A 262 24.01658.513 124.875 1.00 22.73 A ATOM 1954 CB THR A 262 23.734 58.130 126.3321.00 22.38 A ATOM 1955 OG1 THR A 262 22.958 56.927 126.367 1.00 22.08 AATOM 1956 CG2 THR A 262 22.953 59.239 127.022 1.00 22.93 A ATOM 1957 CTHR A 262 24.604 57.320 124.143 1.00 23.97 A ATOM 1958 O THR A 26223.877 56.588 123.464 1.00 24.96 A ATOM 1959 N PHE A 263 25.912 57.122124.260 1.00 22.66 A ATOM 1960 CA PHE A 263 26.541 56.001 123.580 1.0023.58 A ATOM 1961 CB PHE A 263 26.870 56.396 122.144 1.00 23.86 A ATOM1962 CG PHE A 263 27.863 57.515 122.044 1.00 24.17 A ATOM 1963 CD1 PHE A263 29.226 57.249 121.994 1.00 22.87 A ATOM 1964 CD2 PHE A 263 27.43258.840 122.026 1.00 25.32 A ATOM 1965 CE1 PHE A 263 30.153 58.290121.928 1.00 26.00 A ATOM 1966 CE2 PHE A 263 28.348 59.888 121.961 1.0026.02 A ATOM 1967 CZ PHE A 263 29.712 59.613 121.912 1.00 25.32 A ATOM1968 C PHE A 263 27.801 55.525 124.281 1.00 22.97 A ATOM 1969 O PHE A263 28.412 56.253 125.067 1.00 21.66 A ATOM 1970 N TYR A 264 28.17354.283 123.995 1.00 22.70 A ATOM 1971 CA TYR A 264 29.362 53.678 124.5651.00 21.47 A ATOM 1972 CB TYR A 264 28.998 52.613 125.611 1.00 21.41 AATOM 1973 CG TYR A 264 28.038 51.534 125.150 1.00 21.74 A ATOM 1974 CD1TYR A 264 26.662 51.666 125.346 1.00 23.63 A ATOM 1975 CE1 TYR A 26425.775 50.647 124.971 1.00 23.76 A ATOM 1976 CD2 TYR A 264 28.509 50.358124.557 1.00 23.02 A ATOM 1977 CE2 TYR A 264 27.633 49.337 124.178 1.0023.26 A ATOM 1978 CZ TYR A 264 26.267 49.488 124.391 1.00 23.52 A ATOM1979 OH TYR A 264 25.394 48.478 124.041 1.00 21.37 A ATOM 1980 C TYR A264 30.186 53.060 123.447 1.00 22.11 A ATOM 1981 O TYR A 264 29.64852.648 122.418 1.00 22.24 A ATOM 1982 N LEU A 265 31.495 53.014 123.6521.00 23.91 A ATOM 1983 CA LEU A 265 32.421 52.474 122.667 1.00 26.53 AATOM 1984 CB LEU A 265 32.998 53.610 121.815 1.00 28.16 A ATOM 1985 CGLEU A 265 32.020 54.644 121.236 1.00 32.15 A ATOM 1986 CD1 LEU A 26532.800 55.799 120.631 1.00 33.28 A ATOM 1987 CD2 LEU A 265 31.120 54.003120.189 1.00 34.40 A ATOM 1988 C LEU A 265 33.544 51.788 123.432 1.0026.95 A ATOM 1989 O LEU A 265 34.476 52.442 123.901 1.00 28.53 A ATOM1990 N ASN A 266 33.455 50.470 123.566 1.00 26.30 A ATOM 1991 CA ASN A266 34.473 49.731 124.292 1.00 25.13 A ATOM 1992 CB ASN A 266 34.01848.296 124.530 1.00 27.85 A ATOM 1993 CG ASN A 266 34.746 47.651 125.6831.00 30.74 A ATOM 1994 OD1 ASN A 266 34.492 47.971 126.845 1.00 33.50 AATOM 1995 ND2 ASN A 266 35.669 46.750 125.374 1.00 31.85 A ATOM 1996 CASN A 266 35.826 49.712 123.580 1.00 23.31 A ATOM 1997 O ASN A 26635.900 49.755 122.354 1.00 20.14 A ATOM 1998 N LYS A 267 36.896 49.633124.366 1.00 22.48 A ATOM 1999 CA LYS A 267 38.254 49.593 123.832 1.0023.80 A ATOM 2000 CB LYS A 267 39.261 49.664 124.988 1.00 27.81 A ATOM2001 CG LYS A 267 39.011 50.813 125.958 1.00 32.09 A ATOM 2002 CD LYS A267 39.933 50.764 127.182 1.00 35.92 A ATOM 2003 CE LYS A 267 39.61349.595 128.127 1.00 39.38 A ATOM 2004 NZ LYS A 267 40.014 48.253 127.6031.00 40.18 A ATOM 2005 C LYS A 267 38.505 48.311 123.027 1.00 22.43 AATOM 2006 O LYS A 267 39.444 48.232 122.234 1.00 20.97 A ATOM 2007 N SERA 268 37.658 47.310 123.228 1.00 21.81 A ATOM 2008 CA SER A 268 37.81746.029 122.545 1.00 22.21 A ATOM 2009 CB SER A 268 37.109 44.940 123.3421.00 24.17 A ATOM 2010 OG SER A 268 35.709 45.155 123.318 1.00 27.22 AATOM 2011 C SER A 268 37.299 45.985 121.107 1.00 21.22 A ATOM 2012 O SERA 268 37.464 44.974 120.421 1.00 20.98 A ATOM 2013 N VAL A 269 36.68147.067 120.647 1.00 19.08 A ATOM 2014 CA VAL A 269 36.122 47.085 119.3011.00 19.55 A ATOM 2015 CB VAL A 269 35.463 48.454 118.996 1.00 18.98 AATOM 2016 CG1 VAL A 269 35.028 48.515 117.536 1.00 19.74 A ATOM 2017 CG2VAL A 269 34.260 48.652 119.902 1.00 18.22 A ATOM 2018 C VAL A 26937.090 46.698 118.180 1.00 19.21 A ATOM 2019 O VAL A 269 36.813 45.774117.420 1.00 21.42 A ATOM 2020 N PRO A 270 38.235 47.391 118.057 1.0019.54 A ATOM 2021 CD PRO A 270 38.711 48.550 118.833 1.00 19.24 A ATOM2022 CA PRO A 270 39.186 47.047 116.995 1.00 18.50 A ATOM 2023 CB PRO A270 40.388 47.929 117.321 1.00 19.89 A ATOM 2024 CG PRO A 270 39.74349.149 117.915 1.00 19.70 A ATOM 2025 C PRO A 270 39.538 45.557 116.9941.00 19.27 A ATOM 2026 O PRO A 270 39.626 44.917 115.938 1.00 16.45 AATOM 2027 N ASP A 271 39.734 45.007 118.187 1.00 17.58 A ATOM 2028 CAASP A 271 40.071 43.600 118.332 1.00 19.43 A ATOM 2029 CB ASP A 27140.500 43.321 119.785 1.00 23.68 A ATOM 2030 CG ASP A 271 39.756 42.157120.413 1.00 30.76 A ATOM 2031 OD1 ASP A 271 38.543 42.298 120.707 1.0036.55 A ATOM 2032 OD2 ASP A 271 40.383 41.092 120.617 1.00 35.24 A ATOM2033 C ASP A 271 38.924 42.670 117.919 1.00 18.78 A ATOM 2034 O ASP A271 39.154 41.637 117.279 1.00 18.87 A ATOM 2035 N ILE A 272 37.69443.035 118.274 1.00 16.19 A ATOM 2036 CA ILE A 272 36.541 42.209 117.9351.00 16.45 A ATOM 2037 CB ILE A 272 35.247 42.753 118.587 1.00 17.46 AATOM 2038 CG2 ILE A 272 34.056 41.880 118.200 1.00 20.28 A ATOM 2039 CG1ILE A 272 35.403 42.775 120.110 1.00 19.02 A ATOM 2040 CD1 ILE A 27234.200 43.307 120.849 1.00 20.37 A ATOM 2041 C ILE A 272 36.363 42.142116.426 1.00 17.03 A ATOM 2042 O ILE A 272 36.192 41.060 115.856 1.0015.04 A ATOM 2043 N ILE A 273 36.412 43.301 115.777 1.00 17.12 A ATOM2044 CA ILE A 273 36.264 43.369 114.328 1.00 17.75 A ATOM 2045 CB ILE A273 36.243 44.836 113.845 1.00 19.23 A ATOM 2046 CG2 ILE A 273 36.28944.892 112.329 1.00 18.88 A ATOM 2047 CG1 ILE A 273 34.986 45.532114.361 1.00 19.64 A ATOM 2048 CD1 ILE A 273 34.965 47.032 114.095 1.0019.97 A ATOM 2049 C ILE A 273 37.389 42.636 113.597 1.00 19.28 A ATOM2050 O ILE A 273 37.137 41.844 112.684 1.00 18.02 A ATOM 2051 N SER A274 38.631 42.888 113.996 1.00 19.59 A ATOM 2052 CA SER A 274 39.75942.246 113.328 1.00 21.11 A ATOM 2053 CB SER A 274 41.087 42.873 113.7901.00 23.23 A ATOM 2054 OG SER A 274 41.285 42.719 115.183 1.00 22.56 AATOM 2055 C SER A 274 39.783 40.732 113.530 1.00 21.08 A ATOM 2056 O SERA 274 40.322 39.999 112.702 1.00 21.78 A ATOM 2057 N GLN A 275 39.18640.261 114.617 1.00 21.60 A ATOM 2058 CA GLN A 275 39.147 38.824 114.8961.00 22.43 A ATOM 2059 CB GLN A 275 39.056 38.583 116.406 1.00 24.09 AATOM 2060 CG GLN A 275 40.334 38.941 117.162 1.00 28.75 A ATOM 2061 CDGLN A 275 40.235 38.671 118.658 1.00 33.27 A ATOM 2062 OE1 GLN A 27541.170 38.958 119.411 1.00 37.52 A ATOM 2063 NE2 GLN A 275 39.105 38.118119.096 1.00 31.46 A ATOM 2064 C GLN A 275 37.986 38.104 114.196 1.0021.53 A ATOM 2065 O GLN A 275 37.927 36.872 114.178 1.00 21.17 A ATOM2066 N ASN A 276 37.068 38.870 113.620 1.00 19.32 A ATOM 2067 CA ASN A276 35.915 38.279 112.943 1.00 19.41 A ATOM 2068 CB ASN A 276 34.63138.724 113.641 1.00 20.01 A ATOM 2069 CG ASN A 276 34.423 38.029 114.9651.00 20.81 A ATOM 2070 OD1 ASN A 276 33.911 36.911 115.013 1.00 21.49 AATOM 2071 ND2 ASN A 276 34.839 38.677 116.051 1.00 20.50 A ATOM 2072 CASN A 276 35.828 38.635 111.468 1.00 19.52 A ATOM 2073 O ASN A 27634.927 38.170 110.763 1.00 19.26 A ATOM 2074 N ILE A 277 36.763 39.457111.002 1.00 17.49 A ATOM 2075 CA ILE A 277 36.756 39.895 109.613 1.0019.10 A ATOM 2076 CB ILE A 277 37.721 41.093 109.429 1.00 20.08 A ATOM2077 CG2 ILE A 277 39.162 40.614 109.402 1.00 21.44 A ATOM 2078 CG1 ILEA 277 37.369 41.855 108.147 1.00 20.38 A ATOM 2079 CD1 ILE A 277 36.02542.526 108.204 1.00 20.97 A ATOM 2080 C ILE A 277 37.099 38.775 108.6191.00 19.93 A ATOM 2081 O ILE A 277 36.548 38.713 107.520 1.00 18.82 AATOM 2082 N ASN A 278 38.005 37.884 109.002 1.00 19.09 A ATOM 2083 CAASN A 278 38.374 36.795 108.116 1.00 21.07 A ATOM 2084 CB ASN A 27839.536 35.994 108.715 1.00 21.91 A ATOM 2085 CG ASN A 278 40.884 36.662108.491 1.00 25.15 A ATOM 2086 OD1 ASN A 278 41.864 36.352 109.172 1.0029.31 A ATOM 2087 ND2 ASN A 278 40.945 37.569 107.525 1.00 24.39 A ATOM2088 C ASN A 278 37.183 35.883 107.832 1.00 18.75 A ATOM 2089 O ASN A278 36.996 35.446 106.696 1.00 20.29 A ATOM 2090 N ASP A 279 36.37435.600 108.848 1.00 18.61 A ATOM 2091 CA ASP A 279 35.198 34.749 108.6521.00 18.90 A ATOM 2092 CB ASP A 279 34.489 34.482 109.987 1.00 22.33 AATOM 2093 CG ASP A 279 35.247 33.495 110.874 1.00 25.45 A ATOM 2094 OD1ASP A 279 34.914 33.395 112.074 1.00 25.88 A ATOM 2095 OD2 ASP A 27936.166 32.809 110.369 1.00 26.85 A ATOM 2096 C ASP A 279 34.233 35.426107.676 1.00 20.29 A ATOM 2097 O ASP A 279 33.655 34.770 106.808 1.0016.75 A ATOM 2098 N ALA A 280 34.066 36.742 107.813 1.00 17.50 A ATOM2099 CA ALA A 280 33.175 37.487 106.922 1.00 17.54 A ATOM 2100 CB ALA A280 33.037 38.933 107.405 1.00 16.55 A ATOM 2101 C ALA A 280 33.67437.468 105.475 1.00 15.17 A ATOM 2102 O ALA A 280 32.896 37.246 104.5451.00 16.87 A ATOM 2103 N LEU A 281 34.969 37.707 105.288 1.00 14.58 AATOM 2104 CA LEU A 281 35.569 37.715 103.953 1.00 14.95 A ATOM 2105 CBLEU A 281 37.049 38.099 104.033 1.00 14.87 A ATOM 2106 CG LEU A 28137.369 39.579 104.261 1.00 13.37 A ATOM 2107 CD1 LEU A 281 38.829 39.744104.677 1.00 15.16 A ATOM 2108 CD2 LEU A 281 37.082 40.346 102.981 1.0014.81 A ATOM 2109 C LEU A 281 35.445 36.349 103.286 1.00 16.22 A ATOM2110 O LEU A 281 35.119 36.254 102.104 1.00 16.95 A ATOM 2111 N ASN A282 35.712 35.301 104.060 1.00 17.34 A ATOM 2112 CA ASN A 282 35.64133.924 103.582 1.00 18.01 A ATOM 2113 CB ASN A 282 36.099 32.970 104.6871.00 20.09 A ATOM 2114 CG ASN A 282 37.607 32.909 104.825 1.00 22.43 AATOM 2115 OD1 ASN A 282 38.128 32.318 105.772 1.00 23.93 A ATOM 2116 ND2ASN A 282 38.316 33.506 103.877 1.00 22.40 A ATOM 2117 C ASN A 28234.233 33.533 103.140 1.00 18.34 A ATOM 2118 O ASN A 282 34.041 32.933102.078 1.00 17.60 A ATOM 2119 N LYS A 283 33.247 33.861 103.965 1.0017.04 A ATOM 2120 CA LYS A 283 31.865 33.538 103.641 1.00 17.42 A ATOM2121 CB LYS A 283 30.956 33.927 104.809 1.00 17.63 A ATOM 2122 CG LYS A283 29.481 33.667 104.564 1.00 20.90 A ATOM 2123 CD LYS A 283 28.67133.796 105.848 1.00 22.60 A ATOM 2124 CE LYS A 283 27.207 33.456 105.6131.00 23.23 A ATOM 2125 NZ LYS A 283 26.396 33.654 106.842 1.00 21.50 AATOM 2126 C LYS A 283 31.402 34.240 102.361 1.00 16.87 A ATOM 2127 O LYSA 283 30.646 33.681 101.572 1.00 14.25 A ATOM 2128 N ALA A 284 31.87435.464 102.148 1.00 16.88 A ATOM 2129 CA ALA A 284 31.476 36.232 100.9741.00 17.52 A ATOM 2130 CB ALA A 284 31.625 37.733 101.263 1.00 17.75 AATOM 2131 C ALA A 284 32.224 35.879 99.691 1.00 18.24 A ATOM 2132 O ALAA 284 31.629 35.844 98.607 1.00 16.71 A ATOM 2133 N PHE A 285 33.52035.606 99.811 1.00 17.45 A ATOM 2134 CA PHE A 285 34.338 35.314 98.6441.00 18.98 A ATOM 2135 CB PHE A 285 35.633 36.116 98.738 1.00 18.50 AATOM 2136 CG PHE A 285 35.433 37.578 98.496 1.00 16.04 A ATOM 2137 CD1PHE A 285 35.225 38.054 97.206 1.00 17.03 A ATOM 2138 CD2 PHE A 28535.378 38.470 99.559 1.00 16.70 A ATOM 2139 CE1 PHE A 285 34.960 39.40596.976 1.00 15.69 A ATOM 2140 CE2 PHE A 285 35.113 39.819 99.341 1.0015.47 A ATOM 2141 CZ PHE A 285 34.904 40.286 98.053 1.00 15.01 A ATOM2142 C PHE A 285 34.639 33.860 98.300 1.00 19.52 A ATOM 2143 O PHE A 28534.928 33.565 97.144 1.00 21.87 A ATOM 2144 N ASP A 286 34.586 32.95499.273 1.00 21.95 A ATOM 2145 CA ASP A 286 34.837 31.546 98.965 1.0020.77 A ATOM 2146 CB ASP A 286 34.539 30.646 100.169 1.00 23.34 A ATOM2147 CG ASP A 286 35.656 30.642 101.204 1.00 24.33 A ATOM 2148 OD1 ASP A286 36.803 31.013 100.871 1.00 27.05 A ATOM 2149 OD2 ASP A 286 35.38230.247 102.359 1.00 28.19 A ATOM 2150 C ASP A 286 33.972 31.093 97.7791.00 22.10 A ATOM 2151 O ASP A 286 34.462 30.438 96.860 1.00 21.16 AATOM 2152 N PRO A 287 32.671 31.436 97.786 1.00 22.48 A ATOM 2153 CD PROA 287 31.932 32.149 98.842 1.00 23.33 A ATOM 2154 CA PRO A 287 31.76531.049 96.696 1.00 23.96 A ATOM 2155 CB PRO A 287 30.428 31.661 97.1201.00 24.38 A ATOM 2156 CG PRO A 287 30.520 31.683 98.613 1.00 24.07 AATOM 2157 C PRO A 287 32.200 31.567 95.329 1.00 22.69 A ATOM 2158 O PROA 287 31.804 31.030 94.298 1.00 23.56 A ATOM 2159 N LEU A 288 33.01232.617 95.324 1.00 22.92 A ATOM 2160 CA LEU A 288 33.473 33.217 94.0771.00 22.67 A ATOM 2161 CB LEU A 288 33.445 34.740 94.201 1.00 23.12 AATOM 2162 CG LEU A 288 32.092 35.359 94.544 1.00 23.50 A ATOM 2163 CD1LEU A 288 32.286 36.818 94.917 1.00 24.46 A ATOM 2164 CD2 LEU A 28831.147 35.227 93.357 1.00 24.22 A ATOM 2165 C LEU A 288 34.875 32.77293.682 1.00 22.51 A ATOM 2166 O LEU A 288 35.400 33.203 92.656 1.0022.48 A ATOM 2167 N GLY A 289 35.483 31.923 94.506 1.00 22.66 A ATOM2168 CA GLY A 289 36.819 31.445 94.214 1.00 22.32 A ATOM 2169 C GLY A289 37.894 32.502 94.378 1.00 23.21 A ATOM 2170 O GLY A 289 38.91932.451 93.701 1.00 25.59 A ATOM 2171 N ILE A 290 37.668 33.454 95.2811.00 21.89 A ATOM 2172 CA ILE A 290 38.628 34.527 95.536 1.00 21.83 AATOM 2173 CB ILE A 290 37.950 35.909 95.392 1.00 22.82 A ATOM 2174 CG2ILE A 290 38.870 37.006 95.899 1.00 22.10 A ATOM 2175 CG1 ILE A 29037.565 36.135 93.929 1.00 23.68 A ATOM 2176 CD1 ILE A 290 36.795 37.41993.684 1.00 26.43 A ATOM 2177 C ILE A 290 39.210 34.397 96.944 1.0022.08 A ATOM 2178 O ILE A 290 38.467 34.401 97.924 1.00 19.27 A ATOM2179 N SER A 291 40.536 34.297 97.041 1.00 22.84 A ATOM 2180 CA SER A291 41.196 34.150 98.339 1.00 23.66 A ATOM 2181 CB SER A 291 41.87032.777 98.430 1.00 23.67 A ATOM 2182 OG SER A 291 42.768 32.582 97.3551.00 26.92 A ATOM 2183 C SER A 291 42.224 35.241 98.645 1.00 23.75 AATOM 2184 O SER A 291 42.541 35.491 99.811 1.00 22.93 A ATOM 2185 N ASPA 292 42.749 35.875 97.601 1.00 21.84 A ATOM 2186 CA ASP A 292 43.73236.946 97.754 1.00 21.38 A ATOM 2187 CB ASP A 292 44.600 37.027 96.4991.00 23.29 A ATOM 2188 CG ASP A 292 45.573 38.195 96.526 1.00 25.31 AATOM 2189 OD1 ASP A 292 46.344 38.334 95.552 1.00 25.14 A ATOM 2190 OD2ASP A 292 45.568 38.968 97.507 1.00 25.25 A ATOM 2191 C ASP A 292 42.95938.251 97.944 1.00 21.41 A ATOM 2192 O ASP A 292 42.425 38.807 96.9841.00 21.93 A ATOM 2193 N TYR A 293 42.905 38.739 99.177 1.00 18.89 AATOM 2194 CA TYR A 293 42.154 39.956 99.463 1.00 18.84 A ATOM 2195 CBTYR A 293 41.693 39.932 100.924 1.00 19.73 A ATOM 2196 CG TYR A 29340.867 38.694 101.219 1.00 20.84 A ATOM 2197 CD1 TYR A 293 39.776 38.355100.417 1.00 20.08 A ATOM 2198 CE1 TYR A 293 39.041 37.194 100.647 1.0022.81 A ATOM 2199 CD2 TYR A 293 41.199 37.841 102.268 1.00 22.83 A ATOM2200 CE2 TYR A 293 40.472 36.677 102.509 1.00 22.45 A ATOM 2201 CZ TYR A293 39.398 36.359 101.695 1.00 22.48 A ATOM 2202 OH TYR A 293 38.69435.198 101.921 1.00 24.63 A ATOM 2203 C TYR A 293 42.842 41.263 99.0981.00 19.82 A ATOM 2204 O TYR A 293 42.291 42.351 99.306 1.00 17.41 AATOM 2205 N ASN A 294 44.047 41.166 98.538 1.00 18.72 A ATOM 2206 CA ASNA 294 44.733 42.360 98.075 1.00 20.17 A ATOM 2207 CB ASN A 294 46.25142.222 98.206 1.00 19.86 A ATOM 2208 CG ASN A 294 46.758 42.686 99.5501.00 20.29 A ATOM 2209 OD1 ASN A 294 46.625 43.860 99.902 1.00 18.17 AATOM 2210 ND2 ASN A 294 47.338 41.767 100.314 1.00 16.51 A ATOM 2211 CASN A 294 44.364 42.526 96.603 1.00 20.20 A ATOM 2212 O ASN A 294 44.70443.534 95.983 1.00 22.64 A ATOM 2213 N SER A 295 43.661 41.535 96.0521.00 18.20 A ATOM 2214 CA SER A 295 43.269 41.568 94.642 1.00 17.41 AATOM 2215 CB SER A 295 43.334 40.161 94.025 1.00 18.06 A ATOM 2216 OGSER A 295 42.218 39.371 94.403 1.00 19.73 A ATOM 2217 C SER A 295 41.88642.153 94.401 1.00 15.25 A ATOM 2218 O SER A 295 41.413 42.179 93.2631.00 16.23 A ATOM 2219 N ILE A 296 41.227 42.609 95.463 1.00 11.98 AATOM 2220 CA ILE A 296 39.902 43.217 95.328 1.00 13.58 A ATOM 2221 CBILE A 296 38.838 42.449 96.145 1.00 13.48 A ATOM 2222 CG2 ILE A 29638.699 41.018 95.600 1.00 15.53 A ATOM 2223 CG1 ILE A 296 39.233 42.41497.629 1.00 11.74 A ATOM 2224 CD1 ILE A 296 38.169 41.828 98.546 1.0014.12 A ATOM 2225 C ILE A 296 39.992 44.638 95.867 1.00 13.88 A ATOM2226 O ILE A 296 40.947 44.959 96.575 1.00 15.39 A ATOM 2227 N PHE A 29739.029 45.492 95.527 1.00 14.99 A ATOM 2228 CA PHE A 297 39.051 46.84996.064 1.00 15.65 A ATOM 2229 CB PHE A 297 38.472 47.885 95.081 1.0014.57 A ATOM 2230 CG PHE A 297 37.069 47.603 94.611 1.00 15.26 A ATOM2231 CD1 PHE A 297 36.843 46.812 93.487 1.00 15.33 A ATOM 2232 CD2 PHE A297 35.979 48.191 95.244 1.00 15.89 A ATOM 2233 CE1 PHE A 297 35.55446.618 92.996 1.00 15.51 A ATOM 2234 CE2 PHE A 297 34.684 48.005 94.7641.00 16.37 A ATOM 2235 CZ PHE A 297 34.469 47.219 93.636 1.00 16.21 AATOM 2236 C PHE A 297 38.294 46.866 97.383 1.00 15.79 A ATOM 2237 O PHEA 297 37.377 46.063 97.596 1.00 15.96 A ATOM 2238 N TRP A 298 38.67247.792 98.261 1.00 13.76 A ATOM 2239 CA TRP A 298 38.078 47.891 99.5891.00 13.84 A ATOM 2240 CB TRP A 298 39.170 47.690 100.652 1.00 15.00 AATOM 2241 CG TRP A 298 39.590 46.272 100.872 1.00 15.82 A ATOM 2242 CD2TRP A 298 39.394 45.499 102.066 1.00 16.38 A ATOM 2243 CE2 TRP A 29839.943 44.220 101.831 1.00 16.53 A ATOM 2244 CE3 TRP A 298 38.805 45.766103.313 1.00 15.24 A ATOM 2245 CD1 TRP A 298 40.232 45.454 99.986 1.0016.86 A ATOM 2246 NE1 TRP A 298 40.448 44.216 100.556 1.00 16.65 A ATOM2247 CZ2 TRP A 298 39.922 43.204 102.799 1.00 16.35 A ATOM 2248 CZ3 TRPA 298 38.783 44.756 104.275 1.00 17.36 A ATOM 2249 CH2 TRP A 298 39.34243.489 104.009 1.00 16.55 A ATOM 2250 C TRP A 298 37.343 49.181 99.9311.00 15.44 A ATOM 2251 O TRP A 298 37.838 50.274 99.674 1.00 15.12 AATOM 2252 N ILE A 299 36.161 49.033 100.521 1.00 14.10 A ATOM 2253 CAILE A 299 35.367 50.163 100.984 1.00 14.84 A ATOM 2254 CB ILE A 29934.126 50.423 100.098 1.00 12.44 A ATOM 2255 CG2 ILE A 299 33.252 51.511100.741 1.00 12.82 A ATOM 2256 CG1 ILE A 299 34.584 50.866 98.704 1.0011.52 A ATOM 2257 CD1 ILE A 299 33.463 51.004 97.691 1.00 14.86 A ATOM2258 C ILE A 299 34.930 49.777 102.390 1.00 15.35 A ATOM 2259 O ILE A299 34.006 48.991 102.566 1.00 18.17 A ATOM 2260 N ALA A 300 35.61350.316 103.393 1.00 16.48 A ATOM 2261 CA ALA A 300 35.290 49.991 104.7791.00 16.75 A ATOM 2262 CB ALA A 300 36.514 49.376 105.460 1.00 17.74 AATOM 2263 C ALA A 300 34.808 51.191 105.583 1.00 18.52 A ATOM 2264 O ALAA 300 35.309 52.303 105.410 1.00 17.89 A ATOM 2265 N HIS A 301 33.83650.961 106.464 1.00 16.34 A ATOM 2266 CA HIS A 301 33.325 52.024 107.3191.00 17.03 A ATOM 2267 CB HIS A 301 32.164 51.524 108.179 1.00 16.06 AATOM 2268 CG HIS A 301 31.682 52.532 109.179 1.00 17.35 A ATOM 2269 CD2HIS A 301 31.646 52.501 110.533 1.00 18.74 A ATOM 2270 ND1 HIS A 30131.211 53.776 108.813 1.00 18.35 A ATOM 2271 CE1 HIS A 301 30.906 54.468109.897 1.00 18.11 A ATOM 2272 NE2 HIS A 301 31.160 53.718 110.955 1.0018.22 A ATOM 2273 C HIS A 301 34.472 52.467 108.224 1.00 17.49 A ATOM2274 O HIS A 301 35.043 51.655 108.947 1.00 18.95 A ATOM 2275 N PRO A302 34.834 53.760 108.184 1.00 18.79 A ATOM 2276 CD PRO A 302 34.29754.826 107.317 1.00 17.58 A ATOM 2277 CA PRO A 302 35.927 54.261 109.0221.00 18.96 A ATOM 2278 CB PRO A 302 36.359 55.527 108.287 1.00 19.58 AATOM 2279 CG PRO A 302 35.052 56.068 107.800 1.00 19.28 A ATOM 2280 CPRO A 302 35.465 54.544 110.453 1.00 19.81 A ATOM 2281 O PRO A 30235.482 55.691 110.911 1.00 19.60 A ATOM 2282 N GLY A 303 35.044 53.497111.155 1.00 19.20 A ATOM 2283 CA GLY A 303 34.582 53.671 112.521 1.0020.12 A ATOM 2284 C GLY A 303 35.644 54.332 113.377 1.00 23.33 A ATOM2285 O GLY A 303 35.337 55.051 114.333 1.00 23.31 A ATOM 2286 N GLY A304 36.903 54.092 113.019 1.00 23.07 A ATOM 2287 CA GLY A 304 38.01154.668 113.757 1.00 23.38 A ATOM 2288 C GLY A 304 39.348 54.218 113.1991.00 23.14 A ATOM 2289 O GLY A 304 39.438 53.186 112.535 1.00 20.51 AATOM 2290 N ARG A 305 40.387 54.999 113.467 1.00 22.81 A ATOM 2291 CAARG A 305 41.737 54.697 112.997 1.00 23.64 A ATOM 2292 CB ARG A 30542.710 55.725 113.576 1.00 28.06 A ATOM 2293 CG ARG A 305 44.174 55.458113.274 1.00 32.94 A ATOM 2294 CD ARG A 305 45.033 55.993 114.403 1.0037.33 A ATOM 2295 NE ARG A 305 46.429 56.179 114.021 1.00 40.67 A ATOM2296 CZ ARG A 305 47.327 56.795 114.783 1.00 42.66 A ATOM 2297 NH1 ARG A305 46.971 57.280 115.965 1.00 43.64 A ATOM 2298 NH2 ARG A 305 48.57856.938 114.363 1.00 45.35 A ATOM 2299 C ARG A 305 42.197 53.289 113.3921.00 22.76 A ATOM 2300 O ARG A 305 42.684 52.522 112.556 1.00 20.99 AATOM 2301 N ALA A 306 42.037 52.968 114.673 1.00 20.50 A ATOM 2302 CAALA A 306 42.440 51.676 115.224 1.00 20.59 A ATOM 2303 CB ALA A 30642.125 51.638 116.718 1.00 21.66 A ATOM 2304 C ALA A 306 41.804 50.472114.527 1.00 19.21 A ATOM 2305 O ALA A 306 42.460 49.452 114.330 1.0018.90 A ATOM 2306 N ILE A 307 40.523 50.578 114.183 1.00 19.28 A ATOM2307 CA ILE A 307 39.837 49.488 113.496 1.00 17.80 A ATOM 2308 CB ILE A307 38.336 49.810 113.287 1.00 19.27 A ATOM 2309 CG2 ILE A 307 37.67548.727 112.429 1.00 18.14 A ATOM 2310 CG1 ILE A 307 37.639 49.907114.644 1.00 20.87 A ATOM 2311 CD1 ILE A 307 36.228 50.441 114.578 1.0022.85 A ATOM 2312 C ILE A 307 40.489 49.241 112.138 1.00 19.21 A ATOM2313 O ILE A 307 40.796 48.102 111.782 1.00 19.01 A ATOM 2314 N LEU A308 40.709 50.308 111.376 1.00 17.31 A ATOM 2315 CA LEU A 308 41.32650.156 110.069 1.00 18.79 A ATOM 2316 CB LEU A 308 41.352 51.503 109.3291.00 16.84 A ATOM 2317 CG LEU A 308 39.986 52.166 109.093 1.00 16.60 AATOM 2318 CD1 LEU A 308 40.178 53.524 108.421 1.00 15.51 A ATOM 2319 CD2LEU A 308 39.109 51.256 108.237 1.00 17.66 A ATOM 2320 C LEU A 30842.744 49.588 110.203 1.00 17.81 A ATOM 2321 O LEU A 308 43.110 48.655109.486 1.00 18.53 A ATOM 2322 N ASP A 309 43.535 50.134 111.124 1.0018.08 A ATOM 2323 CA ASP A 309 44.900 49.648 111.317 1.00 19.43 A ATOM2324 CB ASP A 309 45.591 50.381 112.476 1.00 19.58 A ATOM 2325 CG ASP A309 45.864 51.850 112.176 1.00 22.23 A ATOM 2326 OD1 ASP A 309 45.63352.295 111.032 1.00 20.80 A ATOM 2327 OD2 ASP A 309 46.319 52.559113.100 1.00 21.47 A ATOM 2328 C ASP A 309 44.924 48.147 111.607 1.0018.66 A ATOM 2329 O ASP A 309 45.695 47.394 110.999 1.00 19.55 A ATOM2330 N GLN A 310 44.079 47.704 112.530 1.00 19.17 A ATOM 2331 CA GLN A310 44.063 46.292 112.893 1.00 19.27 A ATOM 2332 CB GLN A 310 43.33446.107 114.221 1.00 20.83 A ATOM 2333 CG GLN A 310 44.151 46.673 115.3791.00 24.30 A ATOM 2334 CD GLN A 310 43.560 46.375 116.735 1.00 26.80 AATOM 2335 OE1 GLN A 310 43.182 45.239 117.026 1.00 29.98 A ATOM 2336 NE2GLN A 310 43.486 47.393 117.582 1.00 28.79 A ATOM 2337 C GLN A 31043.524 45.344 111.825 1.00 19.13 A ATOM 2338 O GLN A 310 43.979 44.207111.727 1.00 17.24 A ATOM 2339 N VAL A 311 42.576 45.812 111.019 1.0017.16 A ATOM 2340 CA VAL A 311 42.031 44.990 109.948 1.00 17.35 A ATOM2341 CB VAL A 311 40.769 45.643 109.330 1.00 17.80 A ATOM 2342 CG1 VAL A311 40.413 44.973 107.995 1.00 19.45 A ATOM 2343 CG2 VAL A 311 39.60645.506 110.299 1.00 16.82 A ATOM 2344 C VAL A 311 43.115 44.799 108.8811.00 18.13 A ATOM 2345 O VAL A 311 43.300 43.690 108.370 1.00 15.50 AATOM 2346 N GLU A 312 43.841 45.872 108.559 1.00 18.03 A ATOM 2347 CAGLU A 312 44.923 45.801 107.572 1.00 20.30 A ATOM 2348 CB GLU A 31245.571 47.176 107.369 1.00 22.51 A ATOM 2349 CG GLU A 312 44.802 48.102106.456 1.00 27.98 A ATOM 2350 CD GLU A 312 45.431 49.483 106.368 1.0030.36 A ATOM 2351 OE1 GLU A 312 46.632 49.578 106.053 1.00 32.69 A ATOM2352 OE2 GLU A 312 44.721 50.477 106.614 1.00 37.60 A ATOM 2353 C GLU A312 45.998 44.820 108.034 1.00 19.51 A ATOM 2354 O GLU A 312 46.58844.095 107.230 1.00 18.40 A ATOM 2355 N GLN A 313 46.261 44.820 109.3361.00 21.42 A ATOM 2356 CA GLN A 313 47.255 43.932 109.919 1.00 22.77 AATOM 2357 CB GLN A 313 47.501 44.318 111.378 1.00 24.05 A ATOM 2358 CGGLN A 313 48.585 45.356 111.572 1.00 30.88 A ATOM 2359 CD GLN A 31349.975 44.748 111.512 1.00 35.25 A ATOM 2360 OE1 GLN A 313 50.409 44.255110.473 1.00 36.85 A ATOM 2361 NE2 GLN A 313 50.677 44.769 112.639 1.0040.09 A ATOM 2362 C GLN A 313 46.818 42.472 109.837 1.00 21.31 A ATOM2363 O GLN A 313 47.577 41.608 109.399 1.00 22.70 A ATOM 2364 N LYS A314 45.585 42.208 110.249 1.00 21.15 A ATOM 2365 CA LYS A 314 45.04040.855 110.236 1.00 20.71 A ATOM 2366 CB LYS A 314 43.665 40.836 110.9041.00 20.52 A ATOM 2367 CG LYS A 314 43.101 39.443 111.099 1.00 22.86 AATOM 2368 CD LYS A 314 43.948 38.650 112.092 1.00 26.70 A ATOM 2369 CELYS A 314 43.390 37.253 112.316 1.00 28.35 A ATOM 2370 NZ LYS A 31444.240 36.482 113.266 1.00 30.58 A ATOM 2371 C LYS A 314 44.915 40.275108.834 1.00 21.15 A ATOM 2372 O LYS A 314 45.290 39.132 108.596 1.0019.91 A ATOM 2373 N VAL A 315 44.388 41.062 107.902 1.00 20.16 A ATOM2374 CA VAL A 315 44.207 40.589 106.538 1.00 18.60 A ATOM 2375 CB VAL A315 43.032 41.338 105.847 1.00 17.87 A ATOM 2376 CG1 VAL A 315 42.78840.768 104.465 1.00 16.87 A ATOM 2377 CG2 VAL A 315 41.760 41.215106.693 1.00 16.04 A ATOM 2378 C VAL A 315 45.476 40.736 105.699 1.0019.02 A ATOM 2379 O VAL A 315 45.562 40.199 104.595 1.00 18.12 A ATOM2380 N ASN A 316 46.461 41.456 106.235 1.00 19.03 A ATOM 2381 CA ASN A316 47.733 41.683 105.548 1.00 17.21 A ATOM 2382 CB ASN A 316 48.42140.338 105.251 1.00 17.36 A ATOM 2383 CG ASN A 316 49.882 40.499 104.8831.00 18.38 A ATOM 2384 OD1 ASN A 316 50.580 41.357 105.430 1.00 16.26 AATOM 2385 ND2 ASN A 316 50.360 39.665 103.964 1.00 20.02 A ATOM 2386 CASN A 316 47.535 42.481 104.255 1.00 16.62 A ATOM 2387 O ASN A 31648.041 42.110 103.192 1.00 16.59 A ATOM 2388 N LEU A 317 46.811 43.593104.362 1.00 15.63 A ATOM 2389 CA LEU A 317 46.522 44.447 103.212 1.0017.20 A ATOM 2390 CB LEU A 317 45.210 45.212 103.441 1.00 16.66 A ATOM2391 CG LEU A 317 43.936 44.404 103.701 1.00 18.52 A ATOM 2392 CD1 LEU A317 42.778 45.353 104.044 1.00 17.08 A ATOM 2393 CD2 LEU A 317 43.60143.585 102.470 1.00 17.68 A ATOM 2394 C LEU A 317 47.609 45.467 102.9181.00 17.33 A ATOM 2395 O LEU A 317 48.164 46.074 103.836 1.00 17.14 AATOM 2396 N LYS A 318 47.906 45.660 101.637 1.00 16.70 A ATOM 2397 CALYS A 318 48.881 46.665 101.243 1.00 17.06 A ATOM 2398 CB LYS A 31849.074 46.657 99.727 1.00 17.35 A ATOM 2399 CG LYS A 318 49.847 45.44699.211 1.00 18.37 A ATOM 2400 CD LYS A 318 49.921 45.426 97.698 1.0021.60 A ATOM 2401 CE LYS A 318 48.542 45.255 97.074 1.00 24.87 A ATOM2402 NZ LYS A 318 48.600 45.204 95.581 1.00 27.70 A ATOM 2403 C LYS A318 48.261 47.987 101.694 1.00 18.31 A ATOM 2404 O LYS A 318 47.04148.155 101.637 1.00 18.82 A ATOM 2405 N PRO A 319 49.087 48.939 102.1491.00 17.96 A ATOM 2406 CD PRO A 319 50.558 48.856 102.225 1.00 19.64 AATOM 2407 CA PRO A 319 48.625 50.249 102.621 1.00 18.88 A ATOM 2408 CBPRO A 319 49.929 51.020 102.821 1.00 20.93 A ATOM 2409 CG PRO A 31950.885 49.952 103.210 1.00 19.51 A ATOM 2410 C PRO A 319 47.658 51.003101.712 1.00 19.97 A ATOM 2411 O PRO A 319 46.757 51.691 102.195 1.0018.40 A ATOM 2412 N GLU A 320 47.843 50.883 100.401 1.00 21.10 A ATOM2413 CA GLU A 320 46.979 51.588 99.463 1.00 22.71 A ATOM 2414 CB GLU A320 47.555 51.508 98.044 1.00 24.81 A ATOM 2415 CG GLU A 320 48.93952.155 97.890 1.00 33.10 A ATOM 2416 CD GLU A 320 48.985 53.612 98.3391.00 35.66 A ATOM 2417 OE1 GLU A 320 48.827 53.883 99.548 1.00 39.88 AATOM 2418 OE2 GLU A 320 49.184 54.495 97.479 1.00 40.62 A ATOM 2419 CGLU A 320 45.531 51.106 99.464 1.00 20.57 A ATOM 2420 O GLU A 320 44.63151.859 99.105 1.00 18.61 A ATOM 2421 N LYS A 321 45.300 49.863 99.8741.00 18.41 A ATOM 2422 CA LYS A 321 43.941 49.318 99.901 1.00 17.42 AATOM 2423 CB LYS A 321 43.957 47.914 100.525 1.00 18.91 A ATOM 2424 CGLYS A 321 44.603 46.871 99.627 1.00 18.63 A ATOM 2425 CD LYS A 32143.749 46.700 98.385 1.00 23.06 A ATOM 2426 CE LYS A 321 44.484 46.04897.247 1.00 25.54 A ATOM 2427 NZ LYS A 321 43.617 46.071 96.032 1.0022.67 A ATOM 2428 C LYS A 321 42.941 50.216 100.645 1.00 18.06 A ATOM2429 O LYS A 321 41.819 50.436 100.176 1.00 14.96 A ATOM 2430 N MET A322 43.352 50.736 101.800 1.00 17.37 A ATOM 2431 CA MET A 322 42.49651.606 102.613 1.00 16.72 A ATOM 2432 CB MET A 322 42.793 51.380 104.0971.00 18.06 A ATOM 2433 CG MET A 322 42.387 50.017 104.612 1.00 21.77 AATOM 2434 SD MET A 322 40.608 49.856 104.615 1.00 26.83 A ATOM 2435 CEMET A 322 40.379 48.447 105.741 1.00 26.99 A ATOM 2436 C MET A 32242.652 53.099 102.313 1.00 17.42 A ATOM 2437 O MET A 322 42.136 53.940103.055 1.00 14.58 A ATOM 2438 N LYS A 323 43.353 53.439 101.237 1.0016.80 A ATOM 2439 CA LYS A 323 43.570 54.846 100.923 1.00 18.31 A ATOM2440 CB LYS A 323 44.413 54.994 99.654 1.00 20.83 A ATOM 2441 CG LYS A323 44.660 56.440 99.277 1.00 22.34 A ATOM 2442 CD LYS A 323 45.59956.576 98.090 1.00 25.20 A ATOM 2443 CE LYS A 323 45.679 58.028 97.6611.00 27.32 A ATOM 2444 NZ LYS A 323 45.942 58.916 98.833 1.00 27.74 AATOM 2445 C LYS A 323 42.291 55.668 100.788 1.00 18.02 A ATOM 2446 O LYSA 323 42.161 56.717 101.423 1.00 16.95 A ATOM 2447 N ALA A 324 41.34755.207 99.970 1.00 17.17 A ATOM 2448 CA ALA A 324 40.094 55.946 99.7841.00 16.35 A ATOM 2449 CB ALA A 324 39.206 55.241 98.752 1.00 16.45 AATOM 2450 C ALA A 324 39.359 56.070 101.116 1.00 16.75 A ATOM 2451 O ALAA 324 38.813 57.127 101.456 1.00 14.58 A ATOM 2452 N THR A 325 39.35854.984 101.876 1.00 14.25 A ATOM 2453 CA THR A 325 38.699 54.969 103.1741.00 14.58 A ATOM 2454 CB THR A 325 38.752 53.568 103.792 1.00 15.15 AATOM 2455 OG1 THR A 325 37.986 52.670 102.974 1.00 15.01 A ATOM 2456 CG2THR A 325 38.181 53.589 105.205 1.00 13.11 A ATOM 2457 C THR A 32539.314 55.967 104.162 1.00 14.64 A ATOM 2458 O THR A 325 38.601 56.719104.820 1.00 14.11 A ATOM 2459 N ARG A 326 40.636 55.977 104.263 1.0015.97 A ATOM 2460 CA ARG A 326 41.298 56.883 105.194 1.00 14.76 A ATOM2461 CB ARG A 326 42.766 56.485 105.367 1.00 17.17 A ATOM 2462 CG ARG A326 42.970 55.120 106.039 1.00 19.48 A ATOM 2463 CD ARG A 326 44.46254.809 106.181 1.00 21.00 A ATOM 2464 NE ARG A 326 44.729 53.505 106.7891.00 22.68 A ATOM 2465 CZ ARG A 326 44.655 53.237 108.091 1.00 23.59 AATOM 2466 NH1 ARG A 326 44.314 54.181 108.960 1.00 19.97 A ATOM 2467 NH2ARG A 326 44.947 52.018 108.529 1.00 21.31 A ATOM 2468 C ARG A 32641.199 58.343 104.763 1.00 15.95 A ATOM 2469 O ARG A 326 41.204 59.244105.607 1.00 15.73 A ATOM 2470 N ASP A 327 41.116 58.586 103.458 1.0014.52 A ATOM 2471 CA ASP A 327 41.015 59.965 102.974 1.00 16.76 A ATOM2472 CB ASP A 327 41.272 60.025 101.463 1.00 17.65 A ATOM 2473 CG ASP A327 42.758 59.881 101.119 1.00 22.23 A ATOM 2474 OD1 ASP A 327 43.58459.866 102.059 1.00 22.40 A ATOM 2475 OD2 ASP A 327 43.105 59.789 99.9171.00 22.97 A ATOM 2476 C ASP A 327 39.660 60.582 103.331 1.00 15.90 AATOM 2477 O ASP A 327 39.570 61.782 103.623 1.00 16.46 A ATOM 2478 N VALA 328 38.610 59.767 103.317 1.00 14.20 A ATOM 2479 CA VAL A 328 37.27860.247 103.685 1.00 12.95 A ATOM 2480 CB VAL A 328 36.187 59.206 103.3381.00 11.54 A ATOM 2481 CG1 VAL A 328 34.883 59.551 104.045 1.00 13.59 AATOM 2482 CG2 VAL A 328 35.964 59.185 101.824 1.00 12.86 A ATOM 2483 CVAL A 328 37.281 60.513 105.188 1.00 13.33 A ATOM 2484 O VAL A 32836.744 61.519 105.660 1.00 13.72 A ATOM 2485 N LEU A 329 37.899 59.612105.942 1.00 13.61 A ATOM 2486 CA LEU A 329 37.980 59.794 107.380 1.0015.20 A ATOM 2487 CB LEU A 329 38.674 58.594 108.028 1.00 18.20 A ATOM2488 CG LEU A 329 38.996 58.680 109.524 1.00 20.07 A ATOM 2489 CD1 LEU A329 37.723 58.841 110.346 1.00 20.82 A ATOM 2490 CD2 LEU A 329 39.74257.416 109.938 1.00 21.93 A ATOM 2491 C LEU A 329 38.761 61.081 107.6841.00 15.58 A ATOM 2492 O LEU A 329 38.367 61.858 108.543 1.00 16.85 AATOM 2493 N SER A 330 39.859 61.307 106.974 1.00 15.16 A ATOM 2494 CASER A 330 40.663 62.507 107.208 1.00 18.06 A ATOM 2495 CB SER A 33041.946 62.489 106.371 1.00 19.28 A ATOM 2496 OG SER A 330 42.770 61.393106.713 1.00 25.07 A ATOM 2497 C SER A 330 39.933 63.800 106.901 1.0016.71 A ATOM 2498 O SER A 330 40.085 64.787 107.620 1.00 17.70 A ATOM2499 N ASN A 331 39.146 63.791 105.832 1.00 17.19 A ATOM 2500 CA ASN A331 38.434 64.984 105.390 1.00 18.16 A ATOM 2501 CB ASN A 331 38.40265.014 103.858 1.00 20.73 A ATOM 2502 CG ASN A 331 39.792 65.061 103.2511.00 28.36 A ATOM 2503 OD1 ASN A 331 40.259 64.090 102.651 1.00 30.89 AATOM 2504 ND2 ASN A 331 40.465 66.191 103.413 1.00 27.88 A ATOM 2505 CASN A 331 37.019 65.203 105.917 1.00 17.12 A ATOM 2506 O ASN A 33136.514 66.329 105.874 1.00 14.65 A ATOM 2507 N TYR A 332 36.382 64.152106.422 1.00 14.10 A ATOM 2508 CA TYR A 332 35.011 64.284 106.902 1.0015.56 A ATOM 2509 CB TYR A 332 34.056 63.599 105.919 1.00 15.57 A ATOM2510 CG TYR A 332 34.102 64.155 104.522 1.00 16.22 A ATOM 2511 CD1 TYR A332 33.342 65.269 104.165 1.00 17.52 A ATOM 2512 CE1 TYR A 332 33.37865.773 102.865 1.00 19.70 A ATOM 2513 CD2 TYR A 332 34.901 63.562103.547 1.00 17.03 A ATOM 2514 CE2 TYR A 332 34.945 64.055 102.254 1.0018.80 A ATOM 2515 CZ TYR A 332 34.183 65.155 101.919 1.00 20.10 A ATOM2516 OH TYR A 332 34.234 65.629 100.633 1.00 22.65 A ATOM 2517 C TYR A332 34.732 63.728 108.285 1.00 14.80 A ATOM 2518 O TYR A 332 33.71464.056 108.887 1.00 13.27 A ATOM 2519 N GLY A 333 35.618 62.880 108.7921.00 16.28 A ATOM 2520 CA GLY A 333 35.371 62.290 110.090 1.00 16.15 AATOM 2521 C GLY A 333 34.397 61.131 109.935 1.00 18.11 A ATOM 2522 O GLYA 333 34.141 60.682 108.819 1.00 17.58 A ATOM 2523 N ASN A 334 33.84860.660 111.051 1.00 17.54 A ATOM 2524 CA ASN A 334 32.908 59.540 111.0531.00 18.71 A ATOM 2525 CB ASN A 334 33.058 58.749 112.361 1.00 17.01 AATOM 2526 CG ASN A 334 32.251 57.462 112.370 1.00 21.08 A ATOM 2527 OD1ASN A 334 31.230 57.342 111.691 1.00 21.26 A ATOM 2528 ND2 ASN A 33432.700 56.493 113.160 1.00 19.04 A ATOM 2529 C ASN A 334 31.459 60.008110.898 1.00 16.98 A ATOM 2530 O ASN A 334 30.834 60.434 111.867 1.0016.99 A ATOM 2531 N MET A 335 30.931 59.911 109.678 1.00 16.95 A ATOM2532 CA MET A 335 29.559 60.317 109.381 1.00 17.01 A ATOM 2533 CB MET A335 29.506 60.953 107.986 1.00 15.24 A ATOM 2534 CG MET A 335 30.44662.147 107.832 1.00 13.35 A ATOM 2535 SD MET A 335 30.472 62.793 106.1561.00 14.73 A ATOM 2536 CE MET A 335 31.510 61.522 105.336 1.00 11.91 AATOM 2537 C MET A 335 28.552 59.160 109.469 1.00 18.59 A ATOM 2538 O META 335 27.514 59.167 108.806 1.00 17.45 A ATOM 2539 N SER A 336 28.86058.170 110.299 1.00 16.90 A ATOM 2540 CA SER A 336 27.984 57.015 110.4701.00 17.61 A ATOM 2541 CB SER A 336 26.719 57.421 111.241 1.00 19.09 AATOM 2542 OG SER A 336 25.946 56.279 111.582 1.00 22.75 A ATOM 2543 CSER A 336 27.602 56.337 109.144 1.00 16.31 A ATOM 2544 O SER A 33628.465 56.038 108.324 1.00 15.30 A ATOM 2545 N SER A 337 26.313 56.103108.925 1.00 17.61 A ATOM 2546 CA SER A 337 25.875 55.419 107.708 1.0018.36 A ATOM 2547 CB SER A 337 24.351 55.237 107.722 1.00 20.03 A ATOM2548 OG SER A 337 23.682 56.467 107.520 1.00 23.69 A ATOM 2549 C SER A337 26.295 56.038 106.367 1.00 18.79 A ATOM 2550 O SER A 337 26.44155.320 105.378 1.00 19.51 A ATOM 2551 N ALA A 338 26.499 57.352 106.3191.00 16.65 A ATOM 2552 CA ALA A 338 26.879 57.996 105.059 1.00 15.68 AATOM 2553 CB ALA A 338 26.664 59.499 105.162 1.00 15.38 A ATOM 2554 CALA A 338 28.313 57.703 104.595 1.00 16.86 A ATOM 2555 O ALA A 33828.601 57.725 103.396 1.00 14.14 A ATOM 2556 N CYS A 339 29.205 57.409105.540 1.00 17.12 A ATOM 2557 CA CYS A 339 30.611 57.142 105.222 1.0018.43 A ATOM 2558 CB CYS A 339 31.313 56.504 106.420 1.00 20.52 A ATOM2559 SG CYS A 339 31.572 57.633 107.785 1.00 28.72 A ATOM 2560 C CYS A339 30.936 56.309 103.994 1.00 17.20 A ATOM 2561 O CYS A 339 31.58356.789 103.068 1.00 16.64 A ATOM 2562 N VAL A 340 30.507 55.052 103.9861.00 15.01 A ATOM 2563 CA VAL A 340 30.824 54.181 102.865 1.00 15.41 AATOM 2564 CB VAL A 340 30.187 52.785 103.054 1.00 15.58 A ATOM 2565 CG1VAL A 340 30.751 52.143 104.320 1.00 17.48 A ATOM 2566 CG2 VAL A 34028.678 52.900 103.154 1.00 14.74 A ATOM 2567 C VAL A 340 30.449 54.741101.493 1.00 13.89 A ATOM 2568 O VAL A 340 31.066 54.385 100.495 1.0015.42 A ATOM 2569 N PHE A 341 29.456 55.623 101.441 1.00 13.57 A ATOM2570 CA PHE A 341 29.042 56.194 100.161 1.00 12.42 A ATOM 2571 CB PHE A341 27.574 56.622 100.232 1.00 12.79 A ATOM 2572 CG PHE A 341 26.65555.482 100.543 1.00 13.77 A ATOM 2573 CD1 PHE A 341 26.541 54.414 99.6611.00 16.75 A ATOM 2574 CD2 PHE A 341 25.992 55.417 101.763 1.00 17.19 AATOM 2575 CE1 PHE A 341 25.788 53.287 99.992 1.00 17.00 A ATOM 2576 CE2PHE A 341 25.234 54.291 102.108 1.00 18.62 A ATOM 2577 CZ PHE A 34125.137 53.224 101.216 1.00 18.80 A ATOM 2578 C PHE A 341 29.957 57.33499.732 1.00 13.00 A ATOM 2579 O PHE A 341 30.159 57.550 98.537 1.0013.53 A ATOM 2580 N PHE A 342 30.524 58.056 100.698 1.00 13.71 A ATOM2581 CA PHE A 342 31.476 59.116 100.361 1.00 13.53 A ATOM 2582 CB PHE A342 31.854 59.952 101.592 1.00 13.59 A ATOM 2583 CG PHE A 342 30.88061.058 101.907 1.00 14.46 A ATOM 2584 CD1 PHE A 342 29.606 60.776102.386 1.00 12.57 A ATOM 2585 CD2 PHE A 342 31.254 62.388 101.738 1.0017.01 A ATOM 2586 CE1 PHE A 342 28.708 61.813 102.702 1.00 15.37 A ATOM2587 CE2 PHE A 342 30.369 63.429 102.047 1.00 15.22 A ATOM 2588 CZ PHE A342 29.097 63.140 102.531 1.00 14.23 A ATOM 2589 C PHE A 342 32.73158.410 99.836 1.00 12.98 A ATOM 2590 O PHE A 342 33.405 58.895 98.9321.00 11.91 A ATOM 2591 N ILE A 343 33.033 57.248 100.412 1.00 12.62 AATOM 2592 CA ILE A 343 34.201 56.473 100.011 1.00 13.59 A ATOM 2593 CBILE A 343 34.500 55.344 101.038 1.00 12.49 A ATOM 2594 CG2 ILE A 34335.671 54.512 100.561 1.00 12.36 A ATOM 2595 CG1 ILE A 343 34.814 55.964102.412 1.00 14.83 A ATOM 2596 CD1 ILE A 343 34.874 54.980 103.572 1.0013.14 A ATOM 2597 C ILE A 343 33.962 55.868 98.627 1.00 13.20 A ATOM2598 O ILE A 343 34.832 55.911 97.764 1.00 13.62 A ATOM 2599 N MET A 34432.782 55.293 98.427 1.00 13.40 A ATOM 2600 CA MET A 344 32.427 54.72197.131 1.00 13.12 A ATOM 2601 CB MET A 344 31.003 54.157 97.188 1.0014.23 A ATOM 2602 CG MET A 344 30.511 53.546 95.877 1.00 16.48 A ATOM2603 SD MET A 344 28.804 52.931 95.975 1.00 17.54 A ATOM 2604 CE MET A344 29.016 51.477 97.056 1.00 17.01 A ATOM 2605 C MET A 344 32.50655.817 96.060 1.00 11.32 A ATOM 2606 O MET A 344 33.005 55.599 94.9591.00 10.54 A ATOM 2607 N ASP A 345 32.025 57.008 96.399 1.00 12.42 AATOM 2608 CA ASP A 345 32.021 58.121 95.445 1.00 13.38 A ATOM 2609 CBASP A 345 31.203 59.298 96.006 1.00 11.94 A ATOM 2610 CG ASP A 34530.908 60.365 94.957 1.00 19.30 A ATOM 2611 OD1 ASP A 345 30.675 60.00593.781 1.00 17.49 A ATOM 2612 OD2 ASP A 345 30.896 61.566 95.313 1.0022.09 A ATOM 2613 C ASP A 345 33.442 58.557 95.108 1.00 12.01 A ATOM2614 O ASP A 345 33.761 58.776 93.943 1.00 11.34 A ATOM 2615 N LEU A 34634.291 58.669 96.126 1.00 11.80 A ATOM 2616 CA LEU A 346 35.687 59.05595.932 1.00 12.85 A ATOM 2617 CB LEU A 346 36.409 59.176 97.274 1.0012.43 A ATOM 2618 CG LEU A 346 37.879 59.603 97.208 1.00 14.56 A ATOM2619 CD1 LEU A 346 37.981 60.981 96.550 1.00 16.43 A ATOM 2620 CD2 LEU A346 38.462 59.650 98.612 1.00 14.89 A ATOM 2621 C LEU A 346 36.41358.012 95.097 1.00 12.74 A ATOM 2622 O LEU A 346 37.178 58.348 94.1991.00 12.63 A ATOM 2623 N MET A 347 36.172 56.741 95.402 1.00 11.90 AATOM 2624 CA MET A 347 36.832 55.667 94.675 1.00 13.12 A ATOM 2625 CBMET A 347 36.423 54.298 95.223 1.00 15.14 A ATOM 2626 CG MET A 34737.188 53.175 94.563 1.00 13.55 A ATOM 2627 SD MET A 347 36.836 51.53895.229 1.00 18.57 A ATOM 2628 CE MET A 347 37.681 51.612 96.825 1.0016.80 A ATOM 2629 C MET A 347 36.533 55.698 93.185 1.00 13.68 A ATOM2630 O MET A 347 37.449 55.649 92.371 1.00 13.15 A ATOM 2631 N ARG A 34835.258 55.767 92.816 1.00 13.41 A ATOM 2632 CA ARG A 348 34.940 55.79591.398 1.00 13.56 A ATOM 2633 CB ARG A 348 33.434 55.614 91.175 1.0014.13 A ATOM 2634 CG ARG A 348 32.567 56.688 91.771 1.00 16.43 A ATOM2635 CD ARG A 348 31.890 57.508 90.683 1.00 15.10 A ATOM 2636 NE ARG A348 30.971 58.478 91.263 1.00 17.74 A ATOM 2637 CZ ARG A 348 29.94459.021 90.614 1.00 19.42 A ATOM 2638 NH1 ARG A 348 29.692 58.693 89.3501.00 17.83 A ATOM 2639 NH2 ARG A 348 29.161 59.883 91.236 1.00 18.56 AATOM 2640 C ARG A 348 35.440 57.076 90.733 1.00 13.82 A ATOM 2641 O ARGA 348 35.909 57.042 89.596 1.00 12.96 A ATOM 2642 N LYS A 349 35.35258.202 91.436 1.00 14.40 A ATOM 2643 CA LYS A 349 35.815 59.463 90.8661.00 16.03 A ATOM 2644 CB LYS A 349 35.438 60.639 91.779 1.00 19.29 AATOM 2645 CG LYS A 349 33.987 61.107 91.627 1.00 22.73 A ATOM 2646 CDLYS A 349 33.657 62.225 92.615 1.00 25.81 A ATOM 2647 CE LYS A 34932.356 62.941 92.264 1.00 28.02 A ATOM 2648 NZ LYS A 349 31.184 62.03192.147 1.00 29.68 A ATOM 2649 C LYS A 349 37.325 59.441 90.624 1.0016.60 A ATOM 2650 O LYS A 349 37.803 59.892 89.583 1.00 15.58 A ATOM2651 N ARG A 350 38.080 58.917 91.582 1.00 16.64 A ATOM 2652 CA ARG A350 39.527 58.845 91.430 1.00 16.97 A ATOM 2653 CB ARG A 350 40.19158.429 92.738 1.00 19.36 A ATOM 2654 CG ARG A 350 40.260 59.531 93.7681.00 23.11 A ATOM 2655 CD ARG A 350 41.012 59.072 95.001 1.00 25.31 AATOM 2656 NE ARG A 350 41.301 60.187 95.897 1.00 26.05 A ATOM 2657 CZARG A 350 41.851 60.050 97.096 1.00 25.60 A ATOM 2658 NH1 ARG A 35042.174 58.842 97.540 1.00 24.33 A ATOM 2659 NH2 ARG A 350 42.070 61.11897.851 1.00 27.53 A ATOM 2660 C ARG A 350 39.921 57.863 90.342 1.0016.79 A ATOM 2661 O ARG A 350 40.840 58.132 89.574 1.00 15.18 A ATOM2662 N SER A 351 39.237 56.723 90.276 1.00 15.93 A ATOM 2663 CA SER A351 39.559 55.731 89.257 1.00 15.20 A ATOM 2664 CB SER A 351 38.72754.462 89.468 1.00 16.39 A ATOM 2665 OG SER A 351 39.017 53.893 90.7351.00 14.41 A ATOM 2666 C SER A 351 39.316 56.319 87.863 1.00 15.10 AATOM 2667 O SER A 351 40.113 56.122 86.946 1.00 13.78 A ATOM 2668 N LEUA 352 38.221 57.056 87.716 1.00 16.59 A ATOM 2669 CA LEU A 352 37.89757.692 86.444 1.00 18.06 A ATOM 2670 CB LEU A 352 36.540 58.389 86.5411.00 19.15 A ATOM 2671 CG LEU A 352 35.292 57.505 86.519 1.00 19.76 AATOM 2672 CD1 LEU A 352 34.098 58.301 87.018 1.00 21.28 A ATOM 2673 CD2LEU A 352 35.053 56.988 85.112 1.00 21.19 A ATOM 2674 C LEU A 352 38.96958.725 86.097 1.00 19.07 A ATOM 2675 O LEU A 352 39.462 58.779 84.9681.00 17.65 A ATOM 2676 N GLU A 353 39.322 59.540 87.086 1.00 19.59 AATOM 2677 CA GLU A 353 40.320 60.594 86.921 1.00 20.60 A ATOM 2678 CBGLU A 353 40.422 61.400 88.218 1.00 23.38 A ATOM 2679 CG GLU A 35341.485 62.485 88.211 1.00 27.60 A ATOM 2680 CD GLU A 353 41.544 63.23889.530 1.00 29.84 A ATOM 2681 OE1 GLU A 353 41.839 62.606 90.570 1.0031.36 A ATOM 2682 OE2 GLU A 353 41.290 64.460 89.525 1.00 32.62 A ATOM2683 C GLU A 353 41.700 60.070 86.532 1.00 20.58 A ATOM 2684 O GLU A 35342.410 60.696 85.739 1.00 18.53 A ATOM 2685 N GLU A 354 42.075 58.91987.089 1.00 19.90 A ATOM 2686 CA GLU A 354 43.379 58.318 86.823 1.0020.37 A ATOM 2687 CB GLU A 354 43.824 57.507 88.052 1.00 24.66 A ATOM2688 CG GLU A 354 43.839 58.333 89.339 1.00 27.87 A ATOM 2689 CD GLU A354 43.942 57.486 90.598 1.00 31.64 A ATOM 2690 OE1 GLU A 354 43.42756.346 90.602 1.00 31.88 A ATOM 2691 OE2 GLU A 354 44.518 57.972 91.5951.00 32.79 A ATOM 2692 C GLU A 354 43.396 57.437 85.574 1.00 21.48 AATOM 2693 O GLU A 354 44.415 56.819 85.253 1.00 19.63 A ATOM 2694 N GLYA 355 42.268 57.390 84.872 1.00 19.45 A ATOM 2695 CA GLY A 355 42.16656.588 83.664 1.00 21.36 A ATOM 2696 C GLY A 355 42.349 55.093 83.8681.00 21.53 A ATOM 2697 O GLY A 355 42.909 54.419 83.010 1.00 21.87 AATOM 2698 N LEU A 356 41.869 54.569 84.992 1.00 20.13 A ATOM 2699 CA LEUA 356 42.001 53.141 85.289 1.00 20.12 A ATOM 2700 CB LEU A 356 41.77452.898 86.783 1.00 20.13 A ATOM 2701 CG LEU A 356 42.667 53.735 87.7111.00 19.29 A ATOM 2702 CD1 LEU A 356 42.382 53.378 89.163 1.00 19.65 AATOM 2703 CD2 LEU A 356 44.129 53.492 87.381 1.00 19.63 A ATOM 2704 CLEU A 356 41.042 52.287 84.460 1.00 20.67 A ATOM 2705 O LEU A 356 40.15652.817 83.785 1.00 18.66 A ATOM 2706 N LYS A 357 41.218 50.966 84.5231.00 19.35 A ATOM 2707 CA LYS A 357 40.398 50.030 83.754 1.00 19.96 AATOM 2708 CB LYS A 357 41.085 48.663 83.692 1.00 23.34 A ATOM 2709 CGLYS A 357 42.598 48.754 83.565 1.00 30.70 A ATOM 2710 CD LYS A 35743.246 47.382 83.544 1.00 33.70 A ATOM 2711 CE LYS A 357 42.888 46.62382.278 1.00 36.65 A ATOM 2712 NZ LYS A 357 43.583 45.304 82.212 1.0038.22 A ATOM 2713 C LYS A 357 38.979 49.843 84.276 1.00 18.13 A ATOM2714 O LYS A 357 38.084 49.476 83.517 1.00 18.43 A ATOM 2715 N THR A 35838.771 50.068 85.569 1.00 15.16 A ATOM 2716 CA THR A 358 37.442 49.91886.150 1.00 14.31 A ATOM 2717 CB THR A 358 37.243 48.550 86.838 1.0014.13 A ATOM 2718 OG1 THR A 358 37.870 48.575 88.131 1.00 15.36 A ATOM2719 CG2 THR A 358 37.830 47.424 85.995 1.00 14.35 A ATOM 2720 C THR A358 37.218 50.970 87.218 1.00 14.15 A ATOM 2721 O THR A 358 38.16551.593 87.689 1.00 15.99 A ATOM 2722 N THR A 359 35.963 51.132 87.6201.00 13.93 A ATOM 2723 CA THR A 359 35.594 52.101 88.645 1.00 14.78 AATOM 2724 CB THR A 359 34.074 52.257 88.732 1.00 17.18 A ATOM 2725 OG1THR A 359 33.472 50.957 88.692 1.00 16.70 A ATOM 2726 CG2 THR A 35933.544 53.102 87.570 1.00 18.46 A ATOM 2727 C THR A 359 36.095 51.66490.015 1.00 14.99 A ATOM 2728 O THR A 359 36.123 52.459 90.949 1.0014.02 A ATOM 2729 N GLY A 360 36.478 50.395 90.128 1.00 13.30 A ATOM2730 CA GLY A 360 36.970 49.879 91.392 1.00 14.14 A ATOM 2731 C GLY A360 38.486 49.805 91.423 1.00 14.17 A ATOM 2732 O GLY A 360 39.06648.736 91.628 1.00 13.42 A ATOM 2733 N GLU A 361 39.131 50.947 91.2141.00 14.93 A ATOM 2734 CA GLU A 361 40.590 51.025 91.214 1.00 16.26 AATOM 2735 CB GLU A 361 41.131 50.779 92.633 1.00 16.95 A ATOM 2736 CGGLU A 361 40.426 51.624 93.709 1.00 21.62 A ATOM 2737 CD GLU A 36141.057 51.514 95.098 1.00 23.55 A ATOM 2738 OE1 GLU A 361 41.466 50.40395.497 1.00 24.80 A ATOM 2739 OE2 GLU A 361 41.124 52.544 95.804 1.0024.47 A ATOM 2740 C GLU A 361 41.229 50.052 90.210 1.00 15.01 A ATOM2741 O GLU A 361 42.313 49.512 90.437 1.00 14.46 A ATOM 2742 N GLY A 36240.550 49.841 89.089 1.00 13.08 A ATOM 2743 CA GLY A 362 41.071 48.95588.066 1.00 16.80 A ATOM 2744 C GLY A 362 40.894 47.472 88.342 1.0017.02 A ATOM 2745 O GLY A 362 41.318 46.641 87.539 1.00 18.60 A ATOM2746 N LEU A 363 40.281 47.134 89.473 1.00 17.18 A ATOM 2747 CA LEU A363 40.051 45.740 89.827 1.00 18.00 A ATOM 2748 CB LEU A 363 40.38345.514 91.307 1.00 19.02 A ATOM 2749 CG LEU A 363 41.826 45.853 91.6971.00 19.57 A ATOM 2750 CD1 LEU A 363 42.048 45.584 93.180 1.00 20.85 AATOM 2751 CD2 LEU A 363 42.781 45.022 90.863 1.00 22.14 A ATOM 2752 CLEU A 363 38.590 45.367 89.541 1.00 17.57 A ATOM 2753 O LEU A 363 37.71846.238 89.508 1.00 17.19 A ATOM 2754 N ASP A 364 38.323 44.079 89.3321.00 17.36 A ATOM 2755 CA ASP A 364 36.961 43.629 89.030 1.00 17.54 AATOM 2756 CB ASP A 364 36.985 42.329 88.214 1.00 21.31 A ATOM 2757 CGASP A 364 37.599 42.504 86.835 1.00 24.11 A ATOM 2758 OD1 ASP A 36437.602 43.638 86.305 1.00 23.48 A ATOM 2759 OD2 ASP A 364 38.064 41.48786.272 1.00 25.37 A ATOM 2760 C ASP A 364 36.027 43.418 90.226 1.0017.38 A ATOM 2761 O ASP A 364 34.835 43.728 90.143 1.00 15.70 A ATOM2762 N TRP A 365 36.542 42.870 91.324 1.00 14.37 A ATOM 2763 CA TRP A365 35.699 42.634 92.491 1.00 16.23 A ATOM 2764 CB TRP A 365 35.69941.148 92.877 1.00 19.04 A ATOM 2765 CG TRP A 365 35.319 40.238 91.7601.00 22.12 A ATOM 2766 CD2 TRP A 365 34.027 39.675 91.515 1.00 23.55 AATOM 2767 CE2 TRP A 365 34.123 38.908 90.331 1.00 25.41 A ATOM 2768 CE3TRP A 365 32.795 39.745 92.179 1.00 22.91 A ATOM 2769 CD1 TRP A 36536.126 39.803 90.750 1.00 23.60 A ATOM 2770 NE1 TRP A 365 35.415 39.00389.886 1.00 24.40 A ATOM 2771 CZ2 TRP A 365 33.031 38.214 89.794 1.0025.90 A ATOM 2772 CZ3 TRP A 365 31.707 39.054 91.645 1.00 25.49 A ATOM2773 CH2 TRP A 365 31.835 38.299 90.464 1.00 28.06 A ATOM 2774 C TRP A365 36.131 43.449 93.704 1.00 13.48 A ATOM 2775 O TRP A 365 37.30443.791 93.849 1.00 16.37 A ATOM 2776 N GLY A 366 35.170 43.735 94.5751.00 14.49 A ATOM 2777 CA GLY A 366 35.452 44.497 95.774 1.00 15.11 AATOM 2778 C GLY A 366 34.515 44.126 96.907 1.00 14.59 A ATOM 2779 O GLYA 366 33.565 43.361 96.732 1.00 16.03 A ATOM 2780 N VAL A 367 34.79144.674 98.082 1.00 14.23 A ATOM 2781 CA VAL A 367 33.981 44.422 99.2581.00 12.28 A ATOM 2782 CB VAL A 367 34.721 43.482 100.248 1.00 12.07 AATOM 2783 CG1 VAL A 367 35.988 44.156 100.753 1.00 13.16 A ATOM 2784 CG2VAL A 367 33.820 43.111 101.406 1.00 10.94 A ATOM 2785 C VAL A 36733.705 45.749 99.957 1.00 11.97 A ATOM 2786 O VAL A 367 34.550 46.65099.961 1.00 13.50 A ATOM 2787 N LEU A 368 32.510 45.864 100.521 1.0013.10 A ATOM 2788 CA LEU A 368 32.103 47.049 101.273 1.00 14.05 A ATOM2789 CB LEU A 368 30.920 47.755 100.581 1.00 13.70 A ATOM 2790 CG LEU A368 30.298 48.978 101.269 1.00 12.89 A ATOM 2791 CD1 LEU A 368 29.57349.875 100.259 1.00 13.87 A ATOM 2792 CD2 LEU A 368 29.340 48.498102.343 1.00 16.70 A ATOM 2793 C LEU A 368 31.710 46.526 102.652 1.0014.47 A ATOM 2794 O LEU A 368 30.937 45.564 102.760 1.00 15.42 A ATOM2795 N PHE A 369 32.271 47.136 103.697 1.00 15.36 A ATOM 2796 CA PHE A369 32.017 46.735 105.081 1.00 15.36 A ATOM 2797 CB PHE A 369 33.32846.375 105.795 1.00 17.30 A ATOM 2798 CG PHE A 369 33.837 44.996 105.5041.00 16.57 A ATOM 2799 CD1 PHE A 369 33.112 43.875 105.897 1.00 17.75 AATOM 2800 CD2 PHE A 369 35.048 44.817 104.849 1.00 15.72 A ATOM 2801 CE1PHE A 369 33.593 42.587 105.637 1.00 18.32 A ATOM 2802 CE2 PHE A 36935.540 43.533 104.581 1.00 18.65 A ATOM 2803 CZ PHE A 369 34.807 42.415104.978 1.00 17.23 A ATOM 2804 C PHE A 369 31.337 47.787 105.946 1.0017.12 A ATOM 2805 O PHE A 369 31.725 48.964 105.952 1.00 15.30 A ATOM2806 N GLY A 370 30.329 47.345 106.688 1.00 16.03 A ATOM 2807 CA GLY A370 29.650 48.217 107.623 1.00 15.32 A ATOM 2808 C GLY A 370 29.90747.618 109.002 1.00 15.98 A ATOM 2809 O GLY A 370 29.788 46.397 109.1601.00 15.42 A ATOM 2810 N PHE A 371 30.267 48.446 109.986 1.00 15.18 AATOM 2811 CA PHE A 371 30.519 47.969 111.356 1.00 16.88 A ATOM 2812 CBPHE A 371 31.994 48.167 111.748 1.00 16.02 A ATOM 2813 CG PHE A 37132.980 47.576 110.776 1.00 18.36 A ATOM 2814 CD1 PHE A 371 33.002 46.202110.522 1.00 19.96 A ATOM 2815 CD2 PHE A 371 33.899 48.393 110.122 1.0019.62 A ATOM 2816 CE1 PHE A 371 33.925 45.655 109.631 1.00 20.17 A ATOM2817 CE2 PHE A 371 34.827 47.859 109.229 1.00 20.30 A ATOM 2818 CZ PHE A371 34.842 46.484 108.982 1.00 21.44 A ATOM 2819 C PHE A 371 29.64348.749 112.345 1.00 17.73 A ATOM 2820 O PHE A 371 29.607 49.986 112.3111.00 20.57 A ATOM 2821 N GLY A 372 28.959 48.037 113.235 1.00 17.64 AATOM 2822 CA GLY A 372 28.095 48.706 114.193 1.00 18.38 A ATOM 2823 CGLY A 372 27.792 47.924 115.461 1.00 18.00 A ATOM 2824 O GLY A 37228.347 46.860 115.687 1.00 16.36 A ATOM 2825 N PRO A 373 26.887 48.432116.305 1.00 20.27 A ATOM 2826 CD PRO A 373 26.146 49.670 116.005 1.0021.14 A ATOM 2827 CA PRO A 373 26.444 47.861 117.588 1.00 22.67 A ATOM2828 CB PRO A 373 25.456 48.913 118.104 1.00 24.87 A ATOM 2829 CG PRO A373 25.821 50.173 117.373 1.00 23.22 A ATOM 2830 C PRO A 373 25.75346.484 117.592 1.00 23.21 A ATOM 2831 O PRO A 373 25.010 46.202 116.6411.00 22.66 A ATOM 2832 N GLY A 374 26.016 45.617 118.597 1.00 23.17 AATOM 2833 CA GLY A 374 25.178 44.436 118.666 1.00 25.29 A ATOM 2834 CGLY A 374 26.141 43.404 119.175 1.00 23.83 A ATOM 2835 O GLY A 37425.862 42.558 120.092 1.00 25.91 A ATOM 2836 N LEU A 375 27.563 43.367118.304 1.00 24.44 A ATOM 2837 CA LEU A 375 28.323 43.906 117.199 1.0023.26 A ATOM 2838 CB LEU A 375 29.771 44.208 117.541 1.00 23.81 A ATOM2839 CG LEU A 375 30.492 44.899 116.384 1.00 25.97 A ATOM 2840 CD1 LEU A375 31.706 45.711 116.830 1.00 27.70 A ATOM 2841 CD2 LEU A 375 31.00543.917 115.329 1.00 25.62 A ATOM 2842 C LEU A 375 28.226 43.150 115.9071.00 21.89 A ATOM 2843 O LEU A 375 28.728 42.015 115.805 1.00 23.04 AATOM 2844 N THR A 376 27.598 43.904 115.007 1.00 22.34 A ATOM 2845 CATHR A 376 27.220 43.607 113.645 1.00 19.04 A ATOM 2846 CB THR A 37625.952 44.396 113.271 1.00 19.55 A ATOM 2847 OG1 THR A 376 24.994 44.305114.330 1.00 18.35 A ATOM 2848 CG2 THR A 376 25.352 43.860 111.974 1.0019.52 A ATOM 2849 C THR A 376 28.241 44.005 112.607 1.00 18.79 A ATOM2850 O THR A 376 28.837 45.093 112.662 1.00 17.92 A ATOM 2851 N ILE A377 28.406 43.115 111.641 1.00 17.26 A ATOM 2852 CA ILE A 377 29.27743.347 110.513 1.00 17.21 A ATOM 2853 CB ILE A 377 30.458 42.354 110.4731.00 16.53 A ATOM 2854 CG2 ILE A 377 31.241 42.543 109.184 1.00 16.65 AATOM 2855 CG1 ILE A 377 31.367 42.561 111.686 1.00 18.63 A ATOM 2856 CD1ILE A 377 32.527 41.576 111.751 1.00 21.55 A ATOM 2857 C ILE A 37728.400 43.096 109.290 1.00 17.23 A ATOM 2858 O ILE A 377 27.761 42.050109.189 1.00 17.27 A ATOM 2859 N GLU A 378 28.337 44.072 108.393 1.0015.61 A ATOM 2860 CA GLU A 378 27.576 43.934 107.155 1.00 16.65 A ATOM2861 CB GLU A 378 26.732 45.188 106.873 1.00 16.43 A ATOM 2862 CG GLU A378 25.547 45.389 107.813 1.00 20.23 A ATOM 2863 CD GLU A 378 24.20344.968 107.214 1.00 21.67 A ATOM 2864 OE1 GLU A 378 24.176 44.331106.137 1.00 21.94 A ATOM 2865 OE2 GLU A 378 23.163 45.277 107.834 1.0023.26 A ATOM 2866 C GLU A 378 28.641 43.785 106.078 1.00 15.61 A ATOM2867 O GLU A 378 29.575 44.595 106.009 1.00 16.34 A ATOM 2868 N THR A379 28.523 42.743 105.259 1.00 16.22 A ATOM 2869 CA THR A 379 29.49442.504 104.194 1.00 15.92 A ATOM 2870 CB THR A 379 30.224 41.159 104.3781.00 18.24 A ATOM 2871 OG1 THR A 379 30.715 41.052 105.720 1.00 18.54 AATOM 2872 CG2 THR A 379 31.390 41.063 103.404 1.00 17.22 A ATOM 2873 CTHR A 379 28.817 42.460 102.832 1.00 16.86 A ATOM 2874 O THR A 37928.045 41.533 102.540 1.00 16.09 A ATOM 2875 N VAL A 380 29.112 43.450101.997 1.00 12.76 A ATOM 2876 CA VAL A 380 28.534 43.513 100.655 1.0013.53 A ATOM 2877 CB VAL A 380 27.864 44.885 100.401 1.00 13.13 A ATOM2878 CG1 VAL A 380 27.209 44.906 99.009 1.00 14.37 A ATOM 2879 CG2 VAL A380 26.844 45.171 101.483 1.00 14.22 A ATOM 2880 C VAL A 380 29.62043.299 99.597 1.00 14.42 A ATOM 2881 O VAL A 380 30.661 43.958 99.6191.00 13.41 A ATOM 2882 N VAL A 381 29.397 42.362 98.679 1.00 14.62 AATOM 2883 CA VAL A 381 30.374 42.131 97.618 1.00 12.94 A ATOM 2884 CBVAL A 381 30.424 40.663 97.169 1.00 13.15 A ATOM 2885 CG1 VAL A 38131.315 40.537 95.932 1.00 11.65 A ATOM 2886 CG2 VAL A 381 30.962 39.79598.298 1.00 12.83 A ATOM 2887 C VAL A 381 29.962 42.987 96.439 1.0015.10 A ATOM 2888 O VAL A 381 28.787 43.033 96.082 1.00 15.48 A ATOM2889 N LEU A 382 30.935 43.665 95.841 1.00 15.57 A ATOM 2890 CA LEU A382 30.678 44.540 94.707 1.00 15.16 A ATOM 2891 CB LEU A 382 31.11045.971 95.047 1.00 14.71 A ATOM 2892 CG LEU A 382 30.478 46.644 96.2691.00 15.25 A ATOM 2893 CD1 LEU A 382 31.191 47.967 96.546 1.00 16.34 AATOM 2894 CD2 LEU A 382 28.999 46.872 96.024 1.00 16.09 A ATOM 2895 CLEU A 382 31.417 44.114 93.445 1.00 16.18 A ATOM 2896 O LEU A 382 32.43343.423 93.485 1.00 15.42 A ATOM 2897 N ARG A 383 30.893 44.561 92.3131.00 16.91 A ATOM 2898 CA ARG A 383 31.504 44.283 91.039 1.00 18.58 AATOM 2899 CB ARG A 383 30.560 43.438 90.187 1.00 23.70 A ATOM 2900 CGARG A 383 31.212 42.230 89.552 1.00 29.01 A ATOM 2901 CD ARG A 38332.112 42.639 88.406 1.00 34.91 A ATOM 2902 NE ARG A 383 32.578 41.48487.646 1.00 38.99 A ATOM 2903 CZ ARG A 383 33.297 41.570 86.532 1.0041.42 A ATOM 2904 NH1 ARG A 383 33.631 42.760 86.047 1.00 42.61 A ATOM2905 NH2 ARG A 383 33.688 40.468 85.906 1.00 42.22 A ATOM 2906 C ARG A383 31.709 45.663 90.425 1.00 18.51 A ATOM 2907 O ARG A 383 30.79846.493 90.441 1.00 18.35 A ATOM 2908 N SER A 384 32.908 45.918 89.9161.00 17.71 A ATOM 2909 CA SER A 384 33.221 47.205 89.305 1.00 17.18 AATOM 2910 CB SER A 384 34.737 47.429 89.301 1.00 16.78 A ATOM 2911 OGSER A 384 35.377 46.504 88.434 1.00 19.20 A ATOM 2912 C SER A 384 32.70447.244 87.873 1.00 16.69 A ATOM 2913 O SER A 384 32.259 46.231 87.3331.00 14.89 A ATOM 2914 N VAL A 385 32.763 48.422 87.266 1.00 16.95 AATOM 2915 CA VAL A 385 32.318 48.602 85.892 1.00 18.01 A ATOM 2916 CBVAL A 385 31.210 49.679 85.807 1.00 19.03 A ATOM 2917 CG1 VAL A 38530.892 49.986 84.356 1.00 19.61 A ATOM 2918 CG2 VAL A 385 29.968 49.20086.538 1.00 19.12 A ATOM 2919 C VAL A 385 33.503 49.047 85.034 1.0019.45 A ATOM 2920 O VAL A 385 34.277 49.916 85.437 1.00 18.07 A ATOM2921 N ALA A 386 33.637 48.448 83.853 1.00 18.41 A ATOM 2922 CA ALA A386 34.719 48.783 82.937 1.00 19.71 A ATOM 2923 CB ALA A 386 34.69247.833 81.736 1.00 21.24 A ATOM 2924 C ALA A 386 34.633 50.237 82.4591.00 20.60 A ATOM 2925 O ALA A 386 33.573 50.698 82.038 1.00 19.64 AATOM 2926 N ILE A 387 35.757 50.949 82.530 1.00 20.08 A ATOM 2927 CA ILEA 387 35.832 52.344 82.093 1.00 21.90 A ATOM 2928 CB ILE A 387 35.86453.324 83.293 1.00 20.45 A ATOM 2929 CG2 ILE A 387 34.507 53.353 83.9771.00 20.07 A ATOM 2930 CG1 ILE A 387 36.969 52.923 84.274 1.00 20.21 AATOM 2931 CD1 ILE A 387 37.124 53.867 85.451 1.00 17.62 A ATOM 2932 CILE A 387 37.076 52.591 81.233 1.00 23.48 A ATOM 2933 O ILE A 387 37.19053.699 80.664 1.00 24.34 A ATOM 2934 OXT ILE A 387 37.929 51.679 81.1431.00 24.25 A

APPENDIX C 18xCHS Mutant ATOM # TYPE RES X Y Z OCC B ATOM 1 CB VAL A 2−13.230 29.022 69.882 1.00 30.61 A ATOM 2 CG1 VAL A 2 −12.890 29.57971.256 1.00 31.32 A ATOM 3 CG2 VAL A 2 −13.703 27.583 69.999 1.00 31.29A ATOM 4 C VAL A 2 −14.560 29.365 67.801 1.00 29.09 A ATOM 5 O VAL A 2−15.501 28.610 67.557 1.00 29.96 A ATOM 6 N VAL A 2 −15.591 29.84570.002 1.00 30.39 A ATOM 7 CA VAL A 2 −14.326 29.883 69.216 1.00 29.93 AATOM 8 N SER A 3 −13.700 29.774 66.873 1.00 27.49 A ATOM 9 CA SER A 3−13.814 29.352 65.482 1.00 25.81 A ATOM 10 CB SER A 3 −13.481 30.51464.548 1.00 25.39 A ATOM 11 OG SER A 3 −12.104 30.840 64.623 1.00 24.75A ATOM 12 C SER A 3 −12.866 28.195 65.190 1.00 25.08 A ATOM 13 O SER A 3−11.910 27.961 65.931 1.00 24.70 A ATOM 14 N VAL A 4 −13.134 27.47864.102 1.00 24.03 A ATOM 15 CA VAL A 4 −12.298 26.352 63.704 1.00 23.31A ATOM 16 CB VAL A 4 −12.904 25.609 62.491 1.00 23.50 A ATOM 17 CG1 VALA 4 −11.986 24.474 62.058 1.00 23.11 A ATOM 18 CG2 VAL A 4 −14.27525.069 62.848 1.00 23.81 A ATOM 19 C VAL A 4 −10.895 26.833 63.338 1.0022.89 A ATOM 20 O VAL A 4 −9.910 26.129 63.557 1.00 22.82 A ATOM 21 NSER A 5 −10.813 28.037 62.778 1.00 22.60 A ATOM 22 CA SER A 5 −9.52928.613 62.383 1.00 22.06 A ATOM 23 CB SER A 5 −9.742 29.969 61.704 1.0021.99 A ATOM 24 OG SER A 5 −8.505 30.545 61.320 1.00 22.10 A ATOM 25 CSER A 5 −8.610 28.788 63.587 1.00 21.94 A ATOM 26 O SER A 5 −7.43528.423 63.542 1.00 22.12 A ATOM 27 N GLU A 6 −9.151 29.345 64.665 1.0021.69 A ATOM 28 CA GLU A 6 −8.372 29.572 65.875 1.00 21.71 A ATOM 29 CBGLU A 6 −9.195 30.387 66.879 1.00 23.91 A ATOM 30 CG GLU A 6 −8.39030.969 68.040 1.00 28.22 A ATOM 31 CD GLU A 6 −7.384 32.032 67.608 1.0030.05 A ATOM 32 OE1 GLU A 6 −6.670 32.566 68.486 1.00 31.96 A ATOM 33OE2 GLU A 6 −7.302 32.340 66.399 1.00 32.23 A ATOM 34 C GLU A 6 −7.94528.234 66.488 1.00 20.55 A ATOM 35 O GLU A 6 −6.842 28.109 67.019 1.0019.81 A ATOM 36 N ILE A 7 −8.820 27.235 66.402 1.00 18.95 A ATOM 37 CAILE A 7 −8.522 25.909 66.937 1.00 17.56 A ATOM 38 CB ILE A 7 −9.76624.987 66.864 1.00 17.72 A ATOM 39 CG2 ILE A 7 −9.396 23.560 67.269 1.0017.42 A ATOM 40 CG1 ILE A 7 −10.863 25.532 67.784 1.00 17.63 A ATOM 41CD1 ILE A 7 −12.178 24.790 67.693 1.00 17.98 A ATOM 42 C ILE A 7 −7.36725.263 66.169 1.00 16.69 A ATOM 43 O ILE A 7 −6.415 24.767 66.773 1.0016.31 A ATOM 44 N ARG A 8 −7.450 25.283 64.839 1.00 15.59 A ATOM 45 CAARG A 8 −6.411 24.697 63.984 1.00 15.15 A ATOM 46 CB ARG A 8 −6.80324.836 62.506 1.00 14.73 A ATOM 47 CG ARG A 8 −5.829 24.202 61.507 1.0013.64 A ATOM 48 CD ARG A 8 −6.090 22.708 61.297 1.00 13.58 A ATOM 49 NEARG A 8 −5.526 21.844 62.336 1.00 12.35 A ATOM 50 CZ ARG A 8 −4.28421.358 62.326 1.00 13.34 A ATOM 51 NH1 ARG A 8 −3.453 21.644 61.327 1.0012.64 A ATOM 52 NH2 ARG A 8 −3.870 20.578 63.319 1.00 12.49 A ATOM 53 CARG A 8 −5.048 25.359 64.211 1.00 15.17 A ATOM 54 O ARG A 8 −4.02724.678 64.286 1.00 14.78 A ATOM 55 N LYS A 9 −5.034 26.687 64.320 1.0015.05 A ATOM 56 CA LYS A 9 −3.781 27.418 64.528 1.00 15.25 A ATOM 57 CBLYS A 9 −4.039 28.932 64.545 1.00 14.94 A ATOM 58 CG LYS A 9 −4.33229.532 63.178 1.00 15.21 A ATOM 59 CD LYS A 9 −4.522 31.041 63.280 1.0016.42 A ATOM 60 CE LYS A 9 −4.697 31.688 61.910 1.00 16.68 A ATOM 61 NZLYS A 9 −4.801 33.172 62.035 1.00 17.12 A ATOM 62 C LYS A 9 −3.03727.028 65.799 1.00 15.06 A ATOM 63 O LYS A 9 −1.804 27.007 65.822 1.0015.26 A ATOM 64 N ALA A 10 −3.789 26.718 66.852 1.00 15.12 A ATOM 65 CAALA A 10 −3.206 26.349 68.141 1.00 14.75 A ATOM 66 CB ALA A 10 −4.12126.830 69.267 1.00 15.94 A ATOM 67 C ALA A 10 −2.979 24.848 68.268 1.0014.60 A ATOM 68 O ALA A 10 −2.392 24.380 69.248 1.00 14.85 A ATOM 69 NGLN A 11 −3.426 24.099 67.267 1.00 13.64 A ATOM 70 CA GLN A 11 −3.30822.644 67.278 1.00 13.50 A ATOM 71 CB GLN A 11 −4.549 22.038 66.608 1.0012.91 A ATOM 72 CG GLN A 11 −4.852 20.588 66.973 1.00 13.41 A ATOM 73 CDGLN A 11 −6.114 20.076 66.292 1.00 13.72 A ATOM 74 OE1 GLN A 11 −6.10119.746 65.106 1.00 14.06 A ATOM 75 NE2 GLN A 11 −7.214 20.031 67.0361.00 11.82 A ATOM 76 C GLN A 11 −2.048 22.072 66.611 1.00 13.38 A ATOM77 O GLN A 11 −1.550 21.025 67.032 1.00 13.66 A ATOM 78 N ARG A 12−1.531 22.752 65.589 1.00 13.00 A ATOM 79 CA ARG A 12 −0.364 22.25664.850 1.00 12.85 A ATOM 80 CB ARG A 12 −0.338 22.881 63.442 1.00 12.22A ATOM 81 CG ARG A 12 −0.209 24.409 63.409 1.00 12.52 A ATOM 82 CD ARG A12 0.264 24.892 62.036 1.00 13.75 A ATOM 83 NE ARG A 12 −0.672 24.56160.957 1.00 14.03 A ATOM 84 CZ ARG A 12 −1.757 25.271 60.657 1.00 14.40A ATOM 85 NH1 ARG A 12 −2.052 26.364 61.353 1.00 14.54 A ATOM 86 NH2 ARGA 12 −2.549 24.892 59.659 1.00 13.01 A ATOM 87 C ARG A 12 1.022 22.42565.489 1.00 13.09 A ATOM 88 O ARG A 12 1.246 23.329 66.296 1.00 13.33 AATOM 89 N ALA A 13 1.950 21.541 65.116 1.00 13.02 A ATOM 90 CA ALA A 133.333 21.606 65.607 1.00 13.42 A ATOM 91 CB ALA A 13 3.973 20.214 65.5801.00 13.07 A ATOM 92 C ALA A 13 4.078 22.552 64.657 1.00 14.07 A ATOM 93O ALA A 13 3.503 22.988 63.662 1.00 13.68 A ATOM 94 N GLU A 14 5.34222.870 64.938 1.00 15.31 A ATOM 95 CA GLU A 14 6.072 23.788 64.055 1.0016.79 A ATOM 96 CB GLU A 14 6.634 24.983 64.844 1.00 19.19 A ATOM 97 CGGLU A 14 7.664 25.800 64.043 1.00 22.25 A ATOM 98 CD GLU A 14 7.86627.218 64.565 1.00 24.73 A ATOM 99 OE1 GLU A 14 8.977 27.766 64.379 1.0026.12 A ATOM 100 OE2 GLU A 14 6.916 27.794 65.144 1.00 25.41 A ATOM 101C GLU A 14 7.190 23.226 63.180 1.00 16.32 A ATOM 102 O GLU A 14 7.17023.420 61.964 1.00 16.46 A ATOM 103 N GLY A 15 8.162 22.548 63.787 1.0015.23 A ATOM 104 CA GLY A 15 9.282 22.024 63.019 1.00 14.11 A ATOM 105 CGLY A 15 9.151 20.637 62.408 1.00 13.41 A ATOM 106 O GLY A 15 8.10919.999 62.521 1.00 12.54 A ATOM 107 N PRO A 16 10.216 20.142 61.755 1.0012.96 A ATOM 108 CD PRO A 16 11.490 20.849 61.524 1.00 13.60 A ATOM 109CA PRO A 16 10.229 18.821 61.116 1.00 13.35 A ATOM 110 CB PRO A 1611.467 18.892 60.224 1.00 13.76 A ATOM 111 CG PRO A 16 12.407 19.73561.052 1.00 14.19 A ATOM 112 C PRO A 16 10.298 17.666 62.115 1.00 13.11A ATOM 113 O PRO A 16 10.893 17.800 63.188 1.00 13.04 A ATOM 114 N ALA A17 9.685 16.540 61.759 1.00 11.96 A ATOM 115 CA ALA A 17 9.686 15.35562.614 1.00 12.09 A ATOM 116 CB ALA A 17 8.824 14.262 61.993 1.00 11.81A ATOM 117 C ALA A 17 11.119 14.862 62.794 1.00 11.94 A ATOM 118 O ALA A17 11.883 14.766 61.826 1.00 11.18 A ATOM 119 N THR A 18 11.480 14.54364.035 1.00 11.49 A ATOM 120 CA THR A 18 12.834 14.098 64.338 1.00 11.65A ATOM 121 CB THR A 18 13.589 15.190 65.134 1.00 13.41 A ATOM 122 OG1THR A 18 13.434 16.457 64.478 1.00 13.74 A ATOM 123 CG2 THR A 18 15.07214.866 65.228 1.00 14.06 A ATOM 124 C THR A 18 12.850 12.803 65.156 1.0011.14 A ATOM 125 O THR A 18 12.000 12.597 66.023 1.00 11.01 A ATOM 126 NILE A 19 13.810 11.931 64.860 1.00 10.75 A ATOM 127 CA ILE A 19 13.96710.680 65.594 1.00 10.47 A ATOM 128 CB ILE A 19 14.722 9.634 64.757 1.0010.60 A ATOM 129 CG2 ILE A 19 14.941 8.371 65.587 1.00 9.37 A ATOM 130CG1 ILE A 19 13.924 9.327 63.483 1.00 10.89 A ATOM 131 CD1 ILE A 1914.571 8.260 62.584 1.00 12.28 A ATOM 132 C ILE A 19 14.776 11.03466.841 1.00 10.68 A ATOM 133 O ILE A 19 15.886 11.560 66.735 1.00 11.42A ATOM 134 N LEU A 20 14.218 10.745 68.014 1.00 10.93 A ATOM 135 CA LEUA 20 14.850 11.093 69.287 1.00 11.54 A ATOM 136 CB LEU A 20 13.82311.805 70.177 1.00 12.05 A ATOM 137 CG LEU A 20 13.140 13.028 69.5551.00 12.25 A ATOM 138 CD1 LEU A 20 11.991 13.478 70.431 1.00 12.71 AATOM 139 CD2 LEU A 20 14.156 14.157 69.371 1.00 13.13 A ATOM 140 C LEU A20 15.474 9.943 70.072 1.00 11.49 A ATOM 141 O LEU A 20 16.197 10.17771.044 1.00 12.18 A ATOM 142 N ALA A 21 15.194 8.711 69.659 1.00 10.73 AATOM 143 CA ALA A 21 15.731 7.532 70.338 1.00 10.18 A ATOM 144 CB ALA A21 15.087 7.387 71.720 1.00 10.22 A ATOM 145 C ALA A 21 15.456 6.28669.501 1.00 10.69 A ATOM 146 O ALA A 21 14.472 6.242 68.757 1.00 10.07 AATOM 147 N ILE A 22 16.329 5.286 69.622 1.00 10.11 A ATOM 148 CA ILE A22 16.191 4.028 68.885 1.00 10.87 A ATOM 149 CB ILE A 22 17.101 3.99067.624 1.00 11.25 A ATOM 150 CG2 ILE A 22 16.805 2.740 66.807 1.00 10.74A ATOM 151 CG1 ILE A 22 16.889 5.242 66.765 1.00 11.30 A ATOM 152 CD1ILE A 22 17.864 5.344 65.615 1.00 10.46 A ATOM 153 C ILE A 22 16.6022.850 69.766 1.00 11.38 A ATOM 154 O ILE A 22 17.647 2.898 70.415 1.0011.77 A ATOM 155 N GLY A 23 15.778 1.802 69.781 1.00 11.30 A ATOM 156 CAGLY A 23 16.072 0.607 70.560 1.00 11.51 A ATOM 157 C GLY A 23 15.733−0.646 69.760 1.00 12.11 A ATOM 158 O GLY A 23 14.801 −0.614 68.952 1.0011.93 A ATOM 159 N THR A 24 16.482 −1.734 69.961 1.00 11.78 A ATOM 160CA THR A 24 16.244 −2.990 69.239 1.00 11.90 A ATOM 161 CB THR A 2417.278 −3.209 68.094 1.00 12.22 A ATOM 162 OG1 THR A 24 18.587 −3.40768.649 1.00 13.40 A ATOM 163 CG2 THR A 24 17.307 −2.010 67.160 1.0012.77 A ATOM 164 C THR A 24 16.280 −4.234 70.140 1.00 11.99 A ATOM 165 OTHR A 24 16.812 −4.199 71.258 1.00 12.20 A ATOM 166 N ALA A 25 15.713−5.333 69.643 1.00 11.68 A ATOM 167 CA ALA A 25 15.682 −6.596 70.3801.00 11.37 A ATOM 168 CB ALA A 25 14.534 −6.579 71.390 1.00 11.43 A ATOM169 C ALA A 25 15.528 −7.799 69.439 1.00 12.04 A ATOM 170 O ALA A 2514.978 −7.670 68.345 1.00 10.87 A ATOM 171 N ASN A 26 16.020 −8.96469.868 1.00 12.29 A ATOM 172 CA ASN A 26 15.916 −10.194 69.074 1.0012.75 A ATOM 173 CB ASN A 26 17.198 −10.467 68.259 1.00 13.20 A ATOM 174CG ASN A 26 17.652 −9.276 67.425 1.00 13.62 A ATOM 175 OD1 ASN A 2618.349 −8.385 67.919 1.00 13.50 A ATOM 176 ND2 ASN A 26 17.272 −9.26566.145 1.00 11.58 A ATOM 177 C ASN A 26 15.689 −11.396 69.992 1.00 13.37A ATOM 178 O ASN A 26 16.054 −11.366 71.173 1.00 13.18 A ATOM 179 N PROA 27 15.084 −12.474 69.465 1.00 14.48 A ATOM 180 CD PRO A 27 14.417−12.626 68.157 1.00 14.37 A ATOM 181 CA PRO A 27 14.856 −13.652 70.3091.00 15.55 A ATOM 182 CB PRO A 27 14.166 −14.631 69.355 1.00 15.65 AATOM 183 CG PRO A 27 13.383 −13.707 68.445 1.00 14.59 A ATOM 184 C PRO A27 16.203 −14.176 70.820 1.00 16.73 A ATOM 185 O PRO A 27 17.239 −13.96870.185 1.00 16.65 A ATOM 186 N ALA A 28 16.182 −14.861 71.958 1.00 18.08A ATOM 187 CA ALA A 28 17.402 −15.387 72.565 1.00 19.92 A ATOM 188 CBALA A 28 17.091 −15.886 73.983 1.00 20.22 A ATOM 189 C ALA A 28 18.122−16.483 71.771 1.00 20.71 A ATOM 190 O ALA A 28 19.338 −16.634 71.8821.00 22.24 A ATOM 191 N ASN A 29 17.384 −17.239 70.965 1.00 21.91 A ATOM192 CA ASN A 29 17.969 −18.329 70.179 1.00 22.53 A ATOM 193 CB ASN A 2916.853 −19.300 69.770 1.00 23.29 A ATOM 194 CG ASN A 29 17.360 −20.47168.954 1.00 24.78 A ATOM 195 OD1 ASN A 29 18.351 −21.106 69.311 1.0025.80 A ATOM 196 ND2 ASN A 29 16.669 −20.777 67.857 1.00 24.60 A ATOM197 C ASN A 29 18.756 −17.870 68.940 1.00 22.49 A ATOM 198 O ASN A 2918.163 −17.478 67.941 1.00 22.38 A ATOM 199 N CYS A 30 20.088 −17.93069.013 1.00 22.40 A ATOM 200 CA CYS A 30 20.963 −17.534 67.901 1.0023.15 A ATOM 201 CB CYS A 30 22.263 −16.912 68.436 1.00 23.31 A ATOM 202SG CYS A 30 23.478 −16.418 67.155 1.00 25.62 A ATOM 203 C CYS A 3021.297 −18.737 67.012 1.00 23.29 A ATOM 204 O CYS A 30 21.769 −19.76867.496 1.00 23.46 A ATOM 205 N VAL A 31 21.068 −18.590 65.709 1.00 22.78A ATOM 206 CA VAL A 31 21.307 −19.667 64.751 1.00 22.63 A ATOM 207 CBVAL A 31 20.012 −19.961 63.950 1.00 22.87 A ATOM 208 CG1 VAL A 31 20.196−21.191 63.072 1.00 22.78 A ATOM 209 CG2 VAL A 31 18.840 −20.144 64.9071.00 23.17 A ATOM 210 C VAL A 31 22.435 −19.359 63.757 1.00 22.49 A ATOM211 O VAL A 31 22.312 −18.452 62.932 1.00 21.48 A ATOM 212 N GLU A 3223.528 −20.121 63.832 1.00 22.05 A ATOM 213 CA GLU A 32 24.663 −19.92562.925 1.00 22.03 A ATOM 214 CB GLU A 32 25.879 −20.715 63.414 1.0023.60 A ATOM 215 CG GLU A 32 26.500 −20.173 64.690 1.00 25.06 A ATOM 216CD GLU A 32 27.024 −18.765 64.517 1.00 26.01 A ATOM 217 OE1 GLU A 3227.738 −18.520 63.521 1.00 27.39 A ATOM 218 OE2 GLU A 32 26.732 −17.90465.375 1.00 26.48 A ATOM 219 C GLU A 32 24.310 −20.366 61.508 1.00 21.46A ATOM 220 O GLU A 32 23.741 −21.435 61.311 1.00 20.95 A ATOM 221 N GLNA 33 24.672 −19.552 60.521 1.00 20.88 A ATOM 222 CA GLN A 33 24.360−19.853 59.127 1.00 20.56 A ATOM 223 CB GLN A 33 24.497 −18.589 58.2721.00 20.04 A ATOM 224 CG GLN A 33 23.983 −18.751 56.845 1.00 18.89 AATOM 225 CD GLN A 33 22.468 −18.680 56.751 1.00 18.59 A ATOM 226 OE1 GLNA 33 21.751 −19.243 57.581 1.00 17.31 A ATOM 227 NE2 GLN A 33 21.972−17.988 55.726 1.00 17.55 A ATOM 228 C GLN A 33 25.184 −20.974 58.4881.00 20.69 A ATOM 229 O GLN A 33 24.650 −21.768 57.716 1.00 20.26 A ATOM230 N SER A 34 26.475 −21.044 58.801 1.00 21.34 A ATOM 231 CA SER A 3427.331 −22.068 58.201 1.00 22.30 A ATOM 232 CB SER A 34 28.770 −21.95558.732 1.00 21.91 A ATOM 233 OG SER A 34 28.835 −22.155 60.128 1.0022.81 A ATOM 234 C SER A 34 26.822 −23.497 58.383 1.00 22.37 A ATOM 235O SER A 34 27.007 −24.340 57.503 1.00 23.51 A ATOM 236 N THR A 35 26.172−23.772 59.507 1.00 22.43 A ATOM 237 CA THR A 35 25.659 −25.113 59.7651.00 21.81 A ATOM 238 CB THR A 35 26.132 −25.621 61.136 1.00 22.18 AATOM 239 OG1 THR A 35 25.700 −24.714 62.159 1.00 23.03 A ATOM 240 CG2THR A 35 27.651 −25.725 61.165 1.00 22.82 A ATOM 241 C THR A 35 24.133−25.229 59.708 1.00 21.18 A ATOM 242 O THR A 35 23.577 −26.273 60.0561.00 21.01 A ATOM 243 N TYR A 36 23.452 −24.174 59.265 1.00 19.84 A ATOM244 CA TYR A 36 21.991 −24.210 59.196 1.00 18.75 A ATOM 245 CB TYR A 3621.429 −22.843 58.775 1.00 17.52 A ATOM 246 CG TYR A 36 19.928 −22.72158.962 1.00 16.96 A ATOM 247 CD1 TYR A 36 19.346 −22.898 60.220 1.0016.53 A ATOM 248 CE1 TYR A 36 17.964 −22.800 60.397 1.00 16.76 A ATOM249 CD2 TYR A 36 19.088 −22.440 57.881 1.00 16.21 A ATOM 250 CE2 TYR A36 17.705 −22.340 58.047 1.00 15.96 A ATOM 251 CZ TYR A 36 17.149−22.522 59.305 1.00 16.90 A ATOM 252 OH TYR A 36 15.780 −22.438 59.4721.00 16.69 A ATOM 253 C TYR A 36 21.465 −25.294 58.256 1.00 18.74 A ATOM254 O TYR A 36 20.475 −25.955 58.566 1.00 19.06 A ATOM 255 N PRO A 3722.111 −25.489 57.090 1.00 18.99 A ATOM 256 CD PRO A 37 23.208 −24.71756.474 1.00 18.75 A ATOM 257 CA PRO A 37 21.627 −26.525 56.169 1.0018.98 A ATOM 258 CB PRO A 37 22.706 −26.551 55.091 1.00 19.26 A ATOM 259CG PRO A 37 23.097 −25.105 55.005 1.00 18.64 A ATOM 260 C PRO A 3721.424 −27.887 56.838 1.00 19.27 A ATOM 261 O PRO A 37 20.387 −28.52556.653 1.00 18.41 A ATOM 262 N ASP A 38 22.406 −28.331 57.617 1.00 19.51A ATOM 263 CA ASP A 38 22.283 −29.618 58.303 1.00 20.18 A ATOM 264 CBASP A 38 23.582 −29.976 59.040 1.00 20.94 A ATOM 265 CG ASP A 38 24.691−30.417 58.097 1.00 22.36 A ATOM 266 OD1 ASP A 38 24.381 −31.017 57.0431.00 22.82 A ATOM 267 OD2 ASP A 38 25.877 −30.186 58.417 1.00 23.40 AATOM 268 C ASP A 38 21.125 −29.599 59.300 1.00 19.89 A ATOM 269 O ASP A38 20.365 −30.565 59.407 1.00 19.55 A ATOM 270 N PHE A 39 20.991 −28.49260.022 1.00 19.50 A ATOM 271 CA PHE A 39 19.934 −28.340 61.021 1.0019.62 A ATOM 272 CB PHE A 39 20.163 −27.057 61.823 1.00 21.89 A ATOM 273CG PHE A 39 19.139 −26.822 62.892 1.00 24.15 A ATOM 274 CD1 PHE A 3919.106 −27.622 64.031 1.00 25.06 A ATOM 275 CD2 PHE A 39 18.193 −25.81362.753 1.00 25.47 A ATOM 276 CE1 PHE A 39 18.145 −27.423 65.019 1.0026.34 A ATOM 277 CE2 PHE A 39 17.221 −25.603 63.737 1.00 26.52 A ATOM278 CZ PHE A 39 17.198 −26.410 64.871 1.00 27.00 A ATOM 279 C PHE A 3918.535 −28.307 60.400 1.00 18.72 A ATOM 280 O PHE A 39 17.628 −29.01160.852 1.00 18.17 A ATOM 281 N TYR A 40 18.365 −27.484 59.371 1.00 17.64A ATOM 282 CA TYR A 40 17.080 −27.345 58.691 1.00 17.02 A ATOM 283 CBTYR A 40 17.177 −26.240 57.630 1.00 16.06 A ATOM 284 CG TYR A 40 15.923−26.045 56.794 1.00 14.59 A ATOM 285 CD1 TYR A 40 14.742 −25.572 57.3611.00 14.51 A ATOM 286 CE1 TYR A 40 13.595 −25.367 56.585 1.00 14.11 AATOM 287 CD2 TYR A 40 15.933 −26.317 55.430 1.00 14.81 A ATOM 288 CE2TYR A 40 14.799 −26.122 54.646 1.00 14.21 A ATOM 289 CZ TYR A 40 13.635−25.645 55.227 1.00 14.27 A ATOM 290 OH TYR A 40 12.528 −25.435 54.4401.00 13.60 A ATOM 291 C TYR A 40 16.591 −28.647 58.050 1.00 17.25 A ATOM292 O TYR A 40 15.422 −29.004 58.178 1.00 17.01 A ATOM 293 N PHE A 4117.471 −29.363 57.358 1.00 18.01 A ATOM 294 CA PHE A 41 17.044 −30.60756.725 1.00 18.83 A ATOM 295 CB PHE A 41 18.051 −31.035 55.654 1.0018.25 A ATOM 296 CG PHE A 41 17.815 −30.374 54.325 1.00 18.43 A ATOM 297CD1 PHE A 41 18.015 −29.006 54.170 1.00 17.48 A ATOM 298 CD2 PHE A 4117.312 −31.104 53.250 1.00 17.95 A ATOM 299 CE1 PHE A 41 17.713 −28.36952.966 1.00 17.59 A ATOM 300 CE2 PHE A 41 17.006 −30.478 52.046 1.0018.17 A ATOM 301 CZ PHE A 41 17.206 −29.104 51.904 1.00 18.05 A ATOM 302C PHE A 41 16.766 −31.745 57.705 1.00 19.60 A ATOM 303 O PHE A 41 16.048−32.690 57.377 1.00 19.06 A ATOM 304 N LYS A 42 17.314 −31.649 58.9121.00 20.78 A ATOM 305 CA LYS A 42 17.079 −32.678 59.927 1.00 22.23 AATOM 306 CB LYS A 42 18.174 −32.647 60.996 1.00 23.48 A ATOM 307 CG LYSA 42 17.972 −33.680 62.096 1.00 25.67 A ATOM 308 CD LYS A 42 18.923−33.467 63.262 1.00 27.51 A ATOM 309 CE LYS A 42 18.621 −32.169 63.9931.00 29.25 A ATOM 310 NZ LYS A 42 19.511 −31.974 65.173 1.00 30.49 AATOM 311 C LYS A 42 15.724 −32.465 60.608 1.00 22.35 A ATOM 312 O LYS A42 14.909 −33.386 60.697 1.00 22.15 A ATOM 313 N ILE A 43 15.485 −31.24661.085 1.00 22.66 A ATOM 314 CA ILE A 43 14.233 −30.932 61.772 1.0022.68 A ATOM 315 CB ILE A 43 14.269 −29.502 62.372 1.00 22.71 A ATOM 316CG2 ILE A 43 14.054 −28.462 61.282 1.00 21.97 A ATOM 317 CG1 ILE A 4313.190 −29.364 63.446 1.00 23.48 A ATOM 318 CD1 ILE A 43 13.366 −30.31064.624 1.00 23.50 A ATOM 319 C ILE A 43 12.999 −31.082 60.874 1.00 22.84A ATOM 320 O ILE A 43 11.891 −31.309 61.366 1.00 22.92 A ATOM 321 N THRA 44 13.184 −30.960 59.562 1.00 22.55 A ATOM 322 CA THR A 44 12.065−31.104 58.637 1.00 22.54 A ATOM 323 CB THR A 44 12.152 −30.097 57.4591.00 22.72 A ATOM 324 OG1 THR A 44 13.371 −30.303 56.730 1.00 22.37 AATOM 325 CG2 THR A 44 12.098 −28.665 57.977 1.00 22.10 A ATOM 326 C THRA 44 12.014 −32.519 58.071 1.00 23.10 A ATOM 327 O THR A 44 11.202−32.820 57.191 1.00 23.58 A ATOM 328 N ASN A 45 12.887 −33.383 58.5841.00 23.35 A ATOM 329 CA ASN A 45 12.960 −34.775 58.147 1.00 23.44 AATOM 330 CB ASN A 45 11.737 −35.544 58.664 1.00 24.41 A ATOM 331 CG ASNA 45 11.514 −35.346 60.161 1.00 25.94 A ATOM 332 OD1 ASN A 45 12.443−35.452 60.959 1.00 26.60 A ATOM 333 ND2 ASN A 45 10.277 −35.062 60.5441.00 26.55 A ATOM 334 C ASN A 45 13.051 −34.877 56.621 1.00 23.02 A ATOM335 O ASN A 45 12.304 −35.623 55.990 1.00 22.54 A ATOM 336 N SER A 4613.990 −34.133 56.041 1.00 22.98 A ATOM 337 CA SER A 46 14.178 −34.11554.593 1.00 23.29 A ATOM 338 CB SER A 46 13.839 −32.723 54.056 1.0023.17 A ATOM 339 OG SER A 46 12.593 −32.267 54.556 1.00 23.57 A ATOM 340C SER A 46 15.606 −34.483 54.164 1.00 23.38 A ATOM 341 O SER A 46 16.051−34.091 53.086 1.00 22.63 A ATOM 342 N GLU A 47 16.314 −35.241 54.9951.00 23.79 A ATOM 343 CA GLU A 47 17.693 −35.618 54.687 1.00 24.63 AATOM 344 CB GLU A 47 18.342 −36.266 55.912 1.00 25.51 A ATOM 345 CG GLUA 47 18.434 −35.310 57.089 1.00 28.07 A ATOM 346 CD GLU A 47 19.244−35.856 58.236 1.00 29.80 A ATOM 347 OE1 GLU A 47 18.831 −36.878 58.8241.00 31.27 A ATOM 348 OE2 GLU A 47 20.297 −35.260 58.550 1.00 30.37 AATOM 349 C GLU A 47 17.878 −36.510 53.464 1.00 24.72 A ATOM 350 O GLU A47 18.999 −36.670 52.974 1.00 24.73 A ATOM 351 N HIS A 48 16.792 −37.08752.963 1.00 24.76 A ATOM 352 CA HIS A 48 16.893 −37.940 51.785 1.0024.97 A ATOM 353 CB HIS A 48 15.765 −38.978 51.764 1.00 24.66 A ATOM 354CG HIS A 48 14.401 −38.396 51.952 1.00 24.86 A ATOM 355 CD2 HIS A 4813.382 −38.213 51.079 1.00 24.69 A ATOM 356 ND1 HIS A 48 13.956 −37.91953.166 1.00 25.06 A ATOM 357 CE1 HIS A 48 12.721 −37.468 53.033 1.0024.93 A ATOM 358 NE2 HIS A 48 12.350 −37.635 51.777 1.00 24.70 A ATOM359 C HIS A 48 16.870 −37.111 50.502 1.00 25.02 A ATOM 360 O HIS A 4817.084 −37.637 49.411 1.00 24.86 A ATOM 361 N LYS A 49 16.609 −35.81450.634 1.00 25.23 A ATOM 362 CA LYS A 49 16.588 −34.927 49.472 1.0025.72 A ATOM 363 CB LYS A 49 15.576 −33.800 49.680 1.00 26.92 A ATOM 364CG LYS A 49 14.147 −34.284 49.886 1.00 28.26 A ATOM 365 CD LYS A 4913.175 −33.119 49.924 1.00 30.09 A ATOM 366 CE LYS A 49 11.739 −33.59750.099 1.00 31.30 A ATOM 367 NZ LYS A 49 10.776 −32.457 50.099 1.0031.83 A ATOM 368 C LYS A 49 17.993 −34.356 49.298 1.00 25.62 A ATOM 369O LYS A 49 18.215 −33.150 49.423 1.00 25.21 A ATOM 370 N THR A 50 18.936−35.247 49.005 1.00 25.27 A ATOM 371 CA THR A 50 20.344 −34.901 48.8401.00 25.11 A ATOM 372 CB THR A 50 21.147 −36.142 48.410 1.00 25.28 AATOM 373 OG1 THR A 50 20.640 −36.633 47.164 1.00 25.79 A ATOM 374 CG2THR A 50 21.018 −37.238 49.459 1.00 25.39 A ATOM 375 C THR A 50 20.662−33.751 47.882 1.00 25.05 A ATOM 376 O THR A 50 21.462 −32.875 48.2111.00 24.58 A ATOM 377 N GLU A 51 20.054 −33.758 46.700 1.00 24.67 A ATOM378 CA GLU A 51 20.294 −32.703 45.721 1.00 24.81 A ATOM 379 CB GLU A 5119.676 −33.083 44.374 1.00 25.94 A ATOM 380 CG GLU A 51 19.663 −31.96443.338 1.00 27.31 A ATOM 381 CD GLU A 51 20.991 −31.243 43.233 1.0028.46 A ATOM 382 OE1 GLU A 51 22.039 −31.924 43.231 1.00 29.16 A ATOM383 OE2 GLU A 51 20.986 −29.994 43.145 1.00 28.42 A ATOM 384 C GLU A 5119.729 −31.365 46.195 1.00 24.29 A ATOM 385 O GLU A 51 20.385 −30.32846.083 1.00 23.82 A ATOM 386 N LEU A 52 18.511 −31.394 46.725 1.00 23.31A ATOM 387 CA LEU A 52 17.874 −30.180 47.222 1.00 22.68 A ATOM 388 CBLEU A 52 16.477 −30.508 47.767 1.00 22.59 A ATOM 389 CG LEU A 52 15.576−29.339 48.178 1.00 22.20 A ATOM 390 CD1 LEU A 52 15.415 −28.367 47.0161.00 22.61 A ATOM 391 CD2 LEU A 52 14.221 −29.876 48.612 1.00 22.03 AATOM 392 C LEU A 52 18.739 −29.559 48.321 1.00 22.60 A ATOM 393 O LEU A52 18.904 −28.340 48.380 1.00 22.40 A ATOM 394 N LYS A 53 19.299 −30.40149.185 1.00 22.30 A ATOM 395 CA LYS A 53 20.146 −29.916 50.268 1.0022.67 A ATOM 396 CB LYS A 53 20.554 −31.067 51.193 1.00 22.70 A ATOM 397CG LYS A 53 21.340 −30.614 52.422 1.00 23.68 A ATOM 398 CD LYS A 5321.711 −31.786 53.316 1.00 24.89 A ATOM 399 CE LYS A 53 22.373 −31.31254.597 1.00 25.28 A ATOM 400 NZ LYS A 53 22.726 −32.448 55.491 1.0026.32 A ATOM 401 C LYS A 53 21.401 −29.225 49.734 1.00 22.70 A ATOM 402O LYS A 53 21.884 −28.267 50.336 1.00 22.36 A ATOM 403 N GLU A 54 21.933−29.716 48.615 1.00 23.17 A ATOM 404 CA GLU A 54 23.129 −29.112 48.0251.00 23.50 A ATOM 405 CB GLU A 54 23.615 −29.912 46.807 1.00 24.90 AATOM 406 CG GLU A 54 23.970 −31.367 47.092 1.00 27.49 A ATOM 407 CD GLUA 54 24.723 −32.028 45.943 1.00 28.58 A ATOM 408 OE1 GLU A 54 24.314−31.860 44.773 1.00 29.73 A ATOM 409 OE2 GLU A 54 25.723 −32.724 46.2141.00 29.34 A ATOM 410 C GLU A 54 22.793 −27.691 47.591 1.00 22.71 A ATOM411 O GLU A 54 23.573 −26.762 47.814 1.00 22.66 A ATOM 412 N LYS A 5521.629 −27.533 46.964 1.00 21.69 A ATOM 413 CA LYS A 55 21.178 −26.22546.506 1.00 21.03 A ATOM 414 CB LYS A 55 19.819 −26.330 45.801 1.0020.58 A ATOM 415 CG LYS A 55 19.849 −26.920 44.399 1.00 21.67 A ATOM 416CD LYS A 55 18.472 −26.811 43.746 1.00 22.06 A ATOM 417 CE LYS A 5518.490 −27.256 42.290 1.00 22.95 A ATOM 418 NZ LYS A 55 18.862 −28.69242.156 1.00 23.21 A ATOM 419 C LYS A 55 21.049 −25.260 47.684 1.00 20.45A ATOM 420 O LYS A 55 21.441 −24.097 47.588 1.00 19.89 A ATOM 421 N PHEA 56 20.498 −25.748 48.794 1.00 19.90 A ATOM 422 CA PHE A 56 20.309−24.914 49.976 1.00 19.76 A ATOM 423 CB PHE A 56 19.436 −25.638 51.0091.00 19.84 A ATOM 424 CG PHE A 56 18.945 −24.743 52.119 1.00 19.88 AATOM 425 CD1 PHE A 56 18.160 −23.628 51.833 1.00 19.11 A ATOM 426 CD2PHE A 56 19.283 −25.003 53.444 1.00 19.71 A ATOM 427 CE1 PHE A 56 17.718−22.782 52.853 1.00 19.68 A ATOM 428 CE2 PHE A 56 18.848 −24.165 54.4731.00 19.76 A ATOM 429 CZ PHE A 56 18.064 −23.052 54.177 1.00 19.57 AATOM 430 C PHE A 56 21.648 −24.509 50.599 1.00 20.08 A ATOM 431 O PHE A56 21.786 −23.399 51.114 1.00 19.29 A ATOM 432 N GLN A 57 22.633 −25.40450.544 1.00 20.33 A ATOM 433 CA GLN A 57 23.957 −25.102 51.084 1.0021.34 A ATOM 434 CB GLN A 57 24.883 −26.318 50.958 1.00 21.90 A ATOM 435CG GLN A 57 26.264 −26.129 51.590 1.00 22.72 A ATOM 436 CD GLN A 5726.206 −25.936 53.094 1.00 23.02 A ATOM 437 OE1 GLN A 57 25.666 −26.77653.818 1.00 23.90 A ATOM 438 NE2 GLN A 57 26.766 −24.830 53.573 1.0022.69 A ATOM 439 C GLN A 57 24.543 −23.924 50.300 1.00 21.43 A ATOM 440O GLN A 57 25.161 −23.026 50.880 1.00 21.65 A ATOM 441 N ARG A 58 24.344−23.933 48.982 1.00 21.69 A ATOM 442 CA ARG A 58 24.840 −22.857 48.1281.00 22.25 A ATOM 443 CB ARG A 58 24.633 −23.184 46.645 1.00 23.45 AATOM 444 CG ARG A 58 25.478 −24.334 46.108 1.00 27.13 A ATOM 445 CD ARGA 58 25.592 −24.237 44.587 1.00 28.97 A ATOM 446 NE ARG A 58 26.291−25.374 43.994 1.00 31.10 A ATOM 447 CZ ARG A 58 25.779 −26.596 43.8781.00 31.73 A ATOM 448 NH1 ARG A 58 24.551 −26.851 44.316 1.00 30.89 AATOM 449 NH2 ARG A 58 26.495 −27.563 43.317 1.00 31.70 A ATOM 450 C ARGA 58 24.130 −21.544 48.451 1.00 21.39 A ATOM 451 O ARG A 58 24.758−20.487 48.489 1.00 21.08 A ATOM 452 N MET A 59 22.820 −21.616 48.6671.00 20.52 A ATOM 453 CA MET A 59 22.037 −20.433 49.004 1.00 20.06 AATOM 454 CB MET A 59 20.560 −20.801 49.198 1.00 19.96 A ATOM 455 CG META 59 19.825 −21.168 47.908 1.00 20.74 A ATOM 456 SD MET A 59 18.084−21.605 48.175 1.00 20.50 A ATOM 457 CE MET A 59 17.663 −22.339 46.5871.00 21.29 A ATOM 458 C MET A 59 22.586 −19.807 50.285 1.00 20.21 A ATOM459 O MET A 59 22.811 −18.595 50.348 1.00 19.35 A ATOM 460 N CYS A 6022.814 −20.638 51.298 1.00 19.75 A ATOM 461 CA CYS A 60 23.336 −20.15252.571 1.00 20.27 A ATOM 462 CB CYS A 60 23.254 −21.254 53.638 1.0019.75 A ATOM 463 SG CYS A 60 21.564 −21.694 54.177 1.00 19.90 A ATOM 464C CYS A 60 24.772 −19.627 52.468 1.00 20.80 A ATOM 465 O CYS A 60 25.109−18.616 53.085 1.00 20.42 A ATOM 466 N ASP A 61 25.618 −20.301 51.6891.00 21.26 A ATOM 467 CA ASP A 61 27.008 −19.865 51.542 1.00 22.02 AATOM 468 CB ASP A 61 27.826 −20.878 50.729 1.00 22.21 A ATOM 469 CG ASPA 61 28.014 −22.201 51.445 1.00 23.21 A ATOM 470 OD1 ASP A 61 27.908−22.240 52.692 1.00 21.87 A ATOM 471 OD2 ASP A 61 28.290 −23.203 50.7471.00 23.65 A ATOM 472 C ASP A 61 27.161 −18.498 50.875 1.00 22.10 A ATOM473 O ASP A 61 28.122 −17.778 51.145 1.00 22.14 A ATOM 474 N LYS A 6226.224 −18.143 50.004 1.00 22.31 A ATOM 475 CA LYS A 62 26.307 −16.87149.294 1.00 22.65 A ATOM 476 CB LYS A 62 26.114 −17.110 47.797 1.0023.96 A ATOM 477 CG LYS A 62 27.022 −18.201 47.241 1.00 25.71 A ATOM 478CD LYS A 62 27.053 −18.181 45.729 1.00 28.01 A ATOM 479 CE LYS A 6227.778 −16.951 45.218 1.00 29.31 A ATOM 480 NZ LYS A 62 29.179 −16.90645.723 1.00 30.60 A ATOM 481 C LYS A 62 25.331 −15.796 49.768 1.00 22.01A ATOM 482 O LYS A 62 25.206 −14.746 49.135 1.00 21.84 A ATOM 483 N SERA 63 24.660 −16.052 50.886 1.00 20.99 A ATOM 484 CA SER A 63 23.688−15.112 51.438 1.00 20.43 A ATOM 485 CB SER A 63 22.798 −15.830 52.4521.00 19.65 A ATOM 486 OG SER A 63 23.572 −16.299 53.544 1.00 19.58 AATOM 487 C SER A 63 24.326 −13.903 52.118 1.00 20.52 A ATOM 488 O SER A63 23.685 −12.861 52.274 1.00 20.08 A ATOM 489 N MET A 64 25.584 −14.05152.523 1.00 20.87 A ATOM 490 CA MET A 64 26.315 −12.990 53.212 1.0021.59 A ATOM 491 CB MET A 64 26.284 −11.685 52.405 1.00 23.35 A ATOM 492CG MET A 64 26.926 −11.785 51.024 1.00 25.55 A ATOM 493 SD MET A 6428.605 −12.454 51.053 1.00 29.17 A ATOM 494 CE MET A 64 28.299 −14.08550.424 1.00 28.30 A ATOM 495 C MET A 64 25.730 −12.762 54.606 1.00 21.04A ATOM 496 O MET A 64 25.831 −11.671 55.175 1.00 20.22 A ATOM 497 N ILEA 65 25.114 −13.811 55.144 1.00 20.43 A ATOM 498 CA ILE A 65 24.523−13.785 56.478 1.00 19.58 A ATOM 499 CB ILE A 65 23.059 −14.294 56.4571.00 18.89 A ATOM 500 CG2 ILE A 65 22.542 −14.457 57.875 1.00 18.15 AATOM 501 CG1 ILE A 65 22.176 −13.322 55.668 1.00 18.42 A ATOM 502 CD1ILE A 65 20.726 −13.775 55.516 1.00 17.96 A ATOM 503 C ILE A 65 25.344−14.718 57.362 1.00 19.92 A ATOM 504 O ILE A 65 25.572 −15.871 56.9991.00 20.12 A ATOM 505 N LYS A 66 25.794 −14.225 58.513 1.00 19.96 A ATOM506 CA LYS A 66 26.584 −15.047 59.426 1.00 20.16 A ATOM 507 CB LYS A 6627.604 −14.186 60.175 1.00 21.74 A ATOM 508 CG LYS A 66 28.575 −13.46759.257 1.00 24.36 A ATOM 509 CD LYS A 66 29.645 −12.710 60.029 1.0025.33 A ATOM 510 CE LYS A 66 30.637 −13.655 60.689 1.00 26.98 A ATOM 511NZ LYS A 66 31.829 −12.917 61.209 1.00 26.99 A ATOM 512 C LYS A 6625.696 −15.782 60.431 1.00 19.49 A ATOM 513 O LYS A 66 25.986 −16.91860.812 1.00 18.64 A ATOM 514 N ARG A 67 24.622 −15.126 60.861 1.00 18.51A ATOM 515 CA ARG A 67 23.691 −15.726 61.810 1.00 18.88 A ATOM 516 CBARG A 67 24.349 −15.877 63.187 1.00 20.52 A ATOM 517 CG ARG A 67 25.004−14.622 63.746 1.00 23.68 A ATOM 518 CD ARG A 67 25.877 −14.994 64.9461.00 26.21 A ATOM 519 NE ARG A 67 26.647 −13.871 65.476 1.00 28.84 AATOM 520 CZ ARG A 67 27.641 −13.264 64.833 1.00 29.97 A ATOM 521 NH1 ARGA 67 27.999 −13.664 63.621 1.00 30.84 A ATOM 522 NH2 ARG A 67 28.286−12.257 65.410 1.00 30.56 A ATOM 523 C ARG A 67 22.385 −14.950 61.9391.00 17.34 A ATOM 524 O ARG A 67 22.300 −13.788 61.540 1.00 17.53 A ATOM525 N ARG A 68 21.373 −15.612 62.494 1.00 15.84 A ATOM 526 CA ARG A 6820.048 −15.030 62.690 1.00 15.12 A ATOM 527 CB ARG A 68 19.090 −15.51261.595 1.00 15.02 A ATOM 528 CG ARG A 68 19.435 −15.049 60.182 1.0015.37 A ATOM 529 CD ARG A 68 18.539 −15.737 59.159 1.00 15.36 A ATOM 530NE ARG A 68 18.998 −17.087 58.835 1.00 15.15 A ATOM 531 CZ ARG A 6818.294 −17.961 58.118 1.00 16.53 A ATOM 532 NH1 ARG A 68 17.092 −17.63257.656 1.00 14.86 A ATOM 533 NH2 ARG A 68 18.797 −19.160 57.842 1.0015.79 A ATOM 534 C ARG A 68 19.481 −15.459 64.047 1.00 15.54 A ATOM 535O ARG A 68 19.968 −16.408 64.661 1.00 15.15 A ATOM 536 N TYR A 69 18.445−14.762 64.503 1.00 14.96 A ATOM 537 CA TYR A 69 17.798 −15.088 65.7701.00 15.18 A ATOM 538 CB TYR A 69 17.811 −13.869 66.701 1.00 15.19 AATOM 539 CG TYR A 69 19.222 −13.407 67.003 1.00 15.86 A ATOM 540 CD1 TYRA 69 19.938 −12.641 66.081 1.00 15.86 A ATOM 541 CE1 TYR A 69 21.279−12.307 66.304 1.00 16.29 A ATOM 542 CD2 TYR A 69 19.876 −13.821 68.1631.00 16.01 A ATOM 543 CE2 TYR A 69 21.213 −13.498 68.394 1.00 16.51 AATOM 544 CZ TYR A 69 21.909 −12.745 67.462 1.00 16.56 A ATOM 545 OH TYRA 69 23.243 −12.456 67.670 1.00 17.13 A ATOM 546 C TYR A 69 16.377−15.533 65.459 1.00 15.75 A ATOM 547 O TYR A 69 15.668 −14.878 64.6921.00 15.23 A ATOM 548 N MET A 70 15.965 −16.655 66.040 1.00 15.97 A ATOM549 CA MET A 70 14.631 −17.191 65.775 1.00 17.00 A ATOM 550 CB MET A 7014.731 −18.369 64.796 1.00 18.13 A ATOM 551 CG MET A 70 15.216 −18.01963.389 1.00 20.30 A ATOM 552 SD MET A 70 15.414 −19.496 62.341 1.0023.91 A ATOM 553 CE MET A 70 16.362 −18.809 60.972 1.00 22.14 A ATOM 554C MET A 70 13.857 −17.654 67.007 1.00 16.77 A ATOM 555 O MET A 70 14.386−18.385 67.844 1.00 17.33 A ATOM 556 N TYR A 71 12.598 −17.231 67.0991.00 16.96 A ATOM 557 CA TYR A 71 11.713 −17.629 68.193 1.00 17.37 AATOM 558 CB TYR A 71 10.377 −16.878 68.096 1.00 17.57 A ATOM 559 CG TYRA 71 9.219 −17.560 68.802 1.00 18.29 A ATOM 560 CD1 TYR A 71 9.065−17.475 70.185 1.00 18.60 A ATOM 561 CE1 TYR A 71 8.012 −18.126 70.8351.00 19.20 A ATOM 562 CD2 TYR A 71 8.291 −18.311 68.083 1.00 18.96 AATOM 563 CE2 TYR A 71 7.238 −18.963 68.719 1.00 19.52 A ATOM 564 CZ TYRA 71 7.103 −18.868 70.093 1.00 19.82 A ATOM 565 OH TYR A 71 6.056−19.511 70.718 1.00 19.82 A ATOM 566 C TYR A 71 11.462 −19.135 68.0791.00 17.45 A ATOM 567 O TYR A 71 11.358 −19.842 69.085 1.00 16.85 A ATOM568 N LEU A 72 11.348 −19.613 66.843 1.00 17.94 A ATOM 569 CA LEU A 7211.124 −21.032 66.586 1.00 18.87 A ATOM 570 CB LEU A 72 10.858 −21.28865.098 1.00 19.09 A ATOM 571 CG LEU A 72 9.483 −20.991 64.499 1.00 19.52A ATOM 572 CD1 LEU A 72 9.514 −21.350 63.019 1.00 19.49 A ATOM 573 CD2LEU A 72 8.404 −21.791 65.213 1.00 19.42 A ATOM 574 C LEU A 72 12.352−21.831 66.997 1.00 18.91 A ATOM 575 O LEU A 72 13.458 −21.568 66.5281.00 19.47 A ATOM 576 N THR A 73 12.152 −22.808 67.871 1.00 19.15 A ATOM577 CA THR A 73 13.247 −23.651 68.336 1.00 19.69 A ATOM 578 CB THR A 7313.379 −23.592 69.863 1.00 19.91 A ATOM 579 OG1 THR A 73 12.153 −24.03770.457 1.00 20.02 A ATOM 580 CG2 THR A 73 13.679 −22.176 70.321 1.0019.67 A ATOM 581 C THR A 73 12.955 −25.093 67.946 1.00 20.34 A ATOM 582O THR A 73 11.850 −25.416 67.509 1.00 19.94 A ATOM 583 N GLU A 74 13.945−25.963 68.101 1.00 20.84 A ATOM 584 CA GLU A 74 13.747 −27.364 67.7751.00 21.72 A ATOM 585 CB GLU A 74 15.055 −28.140 67.970 1.00 22.75 AATOM 586 CG GLU A 74 14.904 −29.649 67.901 1.00 24.21 A ATOM 587 CD GLUA 74 16.228 −30.359 67.729 1.00 25.53 A ATOM 588 OE1 GLU A 74 17.232−29.907 68.322 1.00 25.87 A ATOM 589 OE2 GLU A 74 16.263 −31.378 67.0031.00 26.84 A ATOM 590 C GLU A 74 12.629 −27.968 68.632 1.00 21.92 A ATOM591 O GLU A 74 11.862 −28.803 68.153 1.00 21.27 A ATOM 592 N GLU A 7512.520 −27.538 69.888 1.00 22.05 A ATOM 593 CA GLU A 75 11.481 −28.07370.769 1.00 22.84 A ATOM 594 CB GLU A 75 11.667 −27.583 72.209 1.0024.92 A ATOM 595 CG GLU A 75 13.096 −27.606 72.704 1.00 27.52 A ATOM 596CD GLU A 75 13.837 −26.334 72.354 1.00 29.08 A ATOM 597 OE1 GLU A 7513.446 −25.259 72.867 1.00 30.76 A ATOM 598 OE2 GLU A 75 14.803 −26.40371.567 1.00 30.32 A ATOM 599 C GLU A 75 10.086 −27.682 70.296 1.00 22.09A ATOM 600 O GLU A 75 9.157 −28.493 70.327 1.00 21.65 A ATOM 601 N ILE A76 9.937 −26.432 69.869 1.00 21.20 A ATOM 602 CA ILE A 76 8.648 −25.95369.388 1.00 20.72 A ATOM 603 CB ILE A 76 8.677 −24.424 69.138 1.00 20.85A ATOM 604 CG2 ILE A 76 7.408 −23.981 68.404 1.00 20.95 A ATOM 605 CG1ILE A 76 8.814 −23.689 70.476 1.00 21.17 A ATOM 606 CD1 ILE A 76 8.900−22.178 70.356 1.00 21.73 A ATOM 607 C ILE A 76 8.288 −26.677 68.0941.00 20.27 A ATOM 608 O ILE A 76 7.169 −27.165 67.939 1.00 19.16 A ATOM609 N LEU A 77 9.243 −26.757 67.173 1.00 20.41 A ATOM 610 CA LEU A 778.992 −27.427 65.904 1.00 21.09 A ATOM 611 CB LEU A 77 10.233 −27.36565.008 1.00 20.90 A ATOM 612 CG LEU A 77 10.516 −25.973 64.424 1.0020.93 A ATOM 613 CD1 LEU A 77 11.852 −25.962 63.711 1.00 21.04 A ATOM614 CD2 LEU A 77 9.395 −25.587 63.467 1.00 20.50 A ATOM 615 C LEU A 778.557 −28.872 66.114 1.00 21.87 A ATOM 616 O LEU A 77 7.678 −29.36765.409 1.00 22.38 A ATOM 617 N LYS A 78 9.150 −29.546 67.095 1.00 22.54A ATOM 618 CA LYS A 78 8.785 −30.933 67.354 1.00 23.21 A ATOM 619 CB LYSA 78 9.792 −31.577 68.320 1.00 24.36 A ATOM 620 CG LYS A 78 11.206−31.602 67.746 1.00 26.62 A ATOM 621 CD LYS A 78 12.031 −32.799 68.2031.00 28.49 A ATOM 622 CE LYS A 78 12.481 −32.672 69.644 1.00 29.78 AATOM 623 NZ LYS A 78 13.422 −33.776 70.010 1.00 30.83 A ATOM 624 C LYS A78 7.355 −31.090 67.871 1.00 22.73 A ATOM 625 O LYS A 78 6.767 −32.16267.753 1.00 23.44 A ATOM 626 N GLU A 79 6.788 −30.017 68.417 1.00 22.50A ATOM 627 CA GLU A 79 5.418 −30.042 68.940 1.00 22.20 A ATOM 628 CB GLUA 79 5.274 −29.037 70.094 1.00 24.23 A ATOM 629 CG GLU A 79 6.191−29.276 71.295 1.00 27.11 A ATOM 630 CD GLU A 79 6.244 −28.080 72.2471.00 29.29 A ATOM 631 OE1 GLU A 79 5.173 −27.543 72.598 1.00 31.41 AATOM 632 OE2 GLU A 79 7.357 −27.678 72.655 1.00 30.28 A ATOM 633 C GLU A79 4.380 −29.695 67.859 1.00 20.87 A ATOM 634 O GLU A 79 3.180 −29.91068.046 1.00 20.47 A ATOM 635 N ASN A 80 4.843 −29.158 66.734 1.00 18.83A ATOM 636 CA ASN A 80 3.946 −28.749 65.648 1.00 17.98 A ATOM 637 CB ASNA 80 4.013 −27.229 65.498 1.00 17.92 A ATOM 638 CG ASN A 80 3.591−26.503 66.761 1.00 18.10 A ATOM 639 OD1 ASN A 80 2.407 −26.251 66.9781.00 17.75 A ATOM 640 ND2 ASN A 80 4.562 −26.178 67.612 1.00 17.68 AATOM 641 C ASN A 80 4.319 −29.421 64.328 1.00 16.94 A ATOM 642 O ASN A80 4.901 −28.797 63.442 1.00 16.43 A ATOM 643 N PRO A 81 3.961 −30.70364.172 1.00 16.48 A ATOM 644 CD PRO A 81 3.181 −31.528 65.108 1.00 16.60A ATOM 645 CA PRO A 81 4.281 −31.448 62.949 1.00 16.06 A ATOM 646 CB PROA 81 3.647 −32.826 63.200 1.00 16.19 A ATOM 647 CG PRO A 81 2.576−32.556 64.195 1.00 17.80 A ATOM 648 C PRO A 81 3.895 −30.837 61.5981.00 15.44 A ATOM 649 O PRO A 81 4.656 −30.956 60.635 1.00 14.88 A ATOM650 N ASN A 82 2.740 −30.180 61.512 1.00 14.66 A ATOM 651 CA ASN A 822.334 −29.578 60.241 1.00 14.83 A ATOM 652 CB ASN A 82 0.833 −29.24060.252 1.00 14.58 A ATOM 653 CG ASN A 82 −0.039 −30.447 59.932 1.0015.49 A ATOM 654 OD1 ASN A 82 −1.277 −30.345 59.864 1.00 15.62 A ATOM655 ND2 ASN A 82 0.598 −31.595 59.729 1.00 14.09 A ATOM 656 C ASN A 823.160 −28.337 59.877 1.00 14.64 A ATOM 657 O ASN A 82 3.217 −27.93958.714 1.00 14.35 A ATOM 658 N VAL A 83 3.805 −27.728 60.866 1.00 14.89A ATOM 659 CA VAL A 83 4.637 −26.556 60.596 1.00 15.18 A ATOM 660 CB VALA 83 5.025 −25.821 61.910 1.00 14.86 A ATOM 661 CG1 VAL A 83 6.039−24.718 61.621 1.00 15.10 A ATOM 662 CG2 VAL A 83 3.783 −25.221 62.5521.00 14.94 A ATOM 663 C VAL A 83 5.909 −26.987 59.857 1.00 15.64 A ATOM664 O VAL A 83 6.543 −26.183 59.162 1.00 15.69 A ATOM 665 N CYS A 846.270 −28.260 59.995 1.00 15.13 A ATOM 666 CA CYS A 84 7.465 −28.79059.341 1.00 16.08 A ATOM 667 CB CYS A 84 8.022 −29.967 60.147 1.00 16.89A ATOM 668 SG CYS A 84 8.593 −29.490 61.809 1.00 20.29 A ATOM 669 C CYSA 84 7.242 −29.216 57.889 1.00 15.77 A ATOM 670 O CYS A 84 8.199 −29.47957.164 1.00 15.77 A ATOM 671 N GLU A 85 5.983 −29.294 57.470 1.00 15.87A ATOM 672 CA GLU A 85 5.658 −29.675 56.098 1.00 16.07 A ATOM 673 CB GLUA 85 4.262 −30.308 56.032 1.00 16.42 A ATOM 674 CG GLU A 85 4.131−31.593 56.834 1.00 16.57 A ATOM 675 CD GLU A 85 4.986 −32.721 56.2801.00 17.93 A ATOM 676 OE1 GLU A 85 5.562 −33.478 57.087 1.00 17.45 AATOM 677 OE2 GLU A 85 5.075 −32.860 55.041 1.00 18.39 A ATOM 678 C GLU A85 5.699 −28.430 55.222 1.00 16.50 A ATOM 679 O GLU A 85 5.616 −27.31655.727 1.00 15.38 A ATOM 680 N TYR A 86 5.830 −28.612 53.910 1.00 17.34A ATOM 681 CA TYR A 86 5.874 −27.460 53.018 1.00 18.46 A ATOM 682 CB TYRA 86 6.224 −27.887 51.582 1.00 19.38 A ATOM 683 CG TYR A 86 6.095−26.761 50.585 1.00 20.22 A ATOM 684 CD1 TYR A 86 6.856 −25.597 50.7161.00 21.14 A ATOM 685 CE1 TYR A 86 6.676 −24.519 49.855 1.00 22.27 AATOM 686 CD2 TYR A 86 5.155 −26.821 49.555 1.00 21.48 A ATOM 687 CE2 TYRA 86 4.967 −25.748 48.686 1.00 22.12 A ATOM 688 CZ TYR A 86 5.727−24.600 48.845 1.00 22.64 A ATOM 689 OH TYR A 86 5.517 −23.521 48.0201.00 23.89 A ATOM 690 C TYR A 86 4.544 −26.712 53.019 1.00 18.72 A ATOM691 O TYR A 86 4.518 −25.482 53.102 1.00 18.89 A ATOM 692 N MET A 873.441 −27.449 52.943 1.00 18.63 A ATOM 693 CA MET A 87 2.128 −26.81852.912 1.00 19.97 A ATOM 694 CB MET A 87 1.734 −26.542 51.463 1.00 22.09A ATOM 695 CG MET A 87 0.665 −25.497 51.318 1.00 24.97 A ATOM 696 SD META 87 1.405 −23.880 51.450 1.00 30.11 A ATOM 697 CE MET A 87 1.541−23.463 49.721 1.00 27.15 A ATOM 698 C MET A 87 1.020 −27.639 53.5741.00 19.37 A ATOM 699 O MET A 87 0.199 −28.245 52.884 1.00 20.41 A ATOM700 N ALA A 88 0.989 −27.654 54.903 1.00 18.05 A ATOM 701 CA ALA A 88−0.033 −28.402 55.642 1.00 17.23 A ATOM 702 CB ALA A 88 0.624 −29.52156.451 1.00 17.03 A ATOM 703 C ALA A 88 −0.797 −27.453 56.576 1.00 16.29A ATOM 704 O ALA A 88 −0.274 −26.407 56.952 1.00 16.42 A ATOM 705 N PROA 89 −2.043 −27.808 56.956 1.00 15.67 A ATOM 706 CD PRO A 89 −2.741−29.042 56.551 1.00 15.28 A ATOM 707 CA PRO A 89 −2.894 −26.998 57.8461.00 15.05 A ATOM 708 CB PRO A 89 −4.104 −27.900 58.083 1.00 15.61 AATOM 709 CG PRO A 89 −4.184 −28.697 56.819 1.00 15.58 A ATOM 710 C PRO A89 −2.178 −26.655 59.154 1.00 14.67 A ATOM 711 O PRO A 89 −1.999 −27.52360.008 1.00 14.71 A ATOM 712 N SER A 90 −1.792 −25.391 59.321 1.00 13.74A ATOM 713 CA SER A 90 −1.061 −24.990 60.526 1.00 13.11 A ATOM 714 CBSER A 90 0.427 −25.292 60.326 1.00 13.29 A ATOM 715 OG SER A 90 0.922−24.652 59.149 1.00 13.45 A ATOM 716 C SER A 90 −1.219 −23.527 60.9501.00 13.09 A ATOM 717 O SER A 90 −0.528 −23.066 61.866 1.00 12.71 A ATOM718 N LEU A 91 −2.125 −22.792 60.309 1.00 12.11 A ATOM 719 CA LEU A 91−2.308 −21.386 60.669 1.00 11.80 A ATOM 720 CB LEU A 91 −3.361 −20.72559.770 1.00 11.33 A ATOM 721 CG LEU A 91 −3.691 −19.275 60.146 1.0011.28 A ATOM 722 CD1 LEU A 91 −2.489 −18.391 59.860 1.00 10.89 A ATOM723 CD2 LEU A 91 −4.913 −18.792 59.357 1.00 10.27 A ATOM 724 C LEU A 91−2.697 −21.164 62.131 1.00 11.83 A ATOM 725 O LEU A 91 −2.109 −20.32162.809 1.00 11.61 A ATOM 726 N ASP A 92 −3.680 −21.917 62.622 1.00 12.12A ATOM 727 CA ASP A 92 −4.134 −21.745 64.001 1.00 12.34 A ATOM 728 CBASP A 92 −5.233 −22.771 64.340 1.00 12.99 A ATOM 729 CG ASP A 92 −6.524−22.550 63.536 1.00 14.23 A ATOM 730 OD1 ASP A 92 −6.606 −21.569 62.7681.00 14.04 A ATOM 731 OD2 ASP A 92 −7.468 −23.362 63.677 1.00 15.03 AATOM 732 C ASP A 92 −2.996 −21.823 65.022 1.00 12.28 A ATOM 733 O ASP A92 −2.963 −21.045 65.980 1.00 12.39 A ATOM 734 N ALA A 93 −2.060 −22.74764.820 1.00 11.80 A ATOM 735 CA ALA A 93 −0.931 −22.884 65.737 1.0011.93 A ATOM 736 CB ALA A 93 −0.177 −24.187 65.462 1.00 12.38 A ATOM 737C ALA A 93 0.010 −21.685 65.601 1.00 12.01 A ATOM 738 O ALA A 93 0.526−21.175 66.599 1.00 11.34 A ATOM 739 N ARG A 94 0.234 −21.237 64.3661.00 11.55 A ATOM 740 CA ARG A 94 1.102 −20.084 64.120 1.00 11.09 A ATOM741 CB ARG A 94 1.325 −19.893 62.605 1.00 10.46 A ATOM 742 CG ARG A 942.047 −21.056 61.875 1.00 10.01 A ATOM 743 CD ARG A 94 1.938 −20.89060.346 1.00 10.88 A ATOM 744 NE ARG A 94 2.397 −22.036 59.544 1.00 11.13A ATOM 745 CZ ARG A 94 3.660 −22.262 59.184 1.00 12.04 A ATOM 746 NH1ARG A 94 4.622 −21.427 59.553 1.00 11.41 A ATOM 747 NH2 ARG A 94 3.962−23.309 58.420 1.00 10.17 A ATOM 748 C ARG A 94 0.484 −18.807 64.7281.00 11.74 A ATOM 749 O ARG A 94 1.201 −17.938 65.236 1.00 12.18 A ATOM750 N GLN A 95 −0.843 −18.699 64.692 1.00 11.95 A ATOM 751 CA GLN A 95−1.524 −17.524 65.243 1.00 12.30 A ATOM 752 CB GLN A 95 −3.039 −17.59064.973 1.00 12.64 A ATOM 753 CG GLN A 95 −3.438 −17.531 63.488 1.0012.78 A ATOM 754 CD GLN A 95 −3.080 −16.212 62.812 1.00 13.00 A ATOM 755OE1 GLN A 95 −1.934 −15.765 62.861 1.00 11.99 A ATOM 756 NE2 GLN A 95−4.067 −15.587 62.170 1.00 12.04 A ATOM 757 C GLN A 95 −1.275 −17.39066.745 1.00 12.26 A ATOM 758 O GLN A 95 −1.037 −16.287 67.243 1.00 11.48A ATOM 759 N ALA A 96 −1.324 −18.511 67.463 1.00 12.75 A ATOM 760 CA ALAA 96 −1.099 −18.502 68.908 1.00 12.75 A ATOM 761 CB ALA A 96 −1.407−19.883 69.503 1.00 12.71 A ATOM 762 C ALA A 96 0.331 −18.085 69.2441.00 12.95 A ATOM 763 O ALA A 96 0.563 −17.420 70.260 1.00 13.08 A ATOM764 N MET A 97 1.284 −18.462 68.389 1.00 12.73 A ATOM 765 CA MET A 972.691 −18.112 68.596 1.00 12.42 A ATOM 766 CB MET A 97 3.597 −18.84967.596 1.00 12.18 A ATOM 767 CG MET A 97 3.612 −20.371 67.718 1.00 11.76A ATOM 768 SD MET A 97 4.617 −21.149 66.408 1.00 13.63 A ATOM 769 CE META 97 4.109 −22.880 66.555 1.00 12.10 A ATOM 770 C MET A 97 2.899 −16.60968.423 1.00 12.57 A ATOM 771 O MET A 97 3.570 −15.962 69.236 1.00 12.06A ATOM 772 N LEU A 98 2.328 −16.062 67.354 1.00 11.79 A ATOM 773 CA LEUA 98 2.452 −14.634 67.063 1.00 12.16 A ATOM 774 CB LEU A 98 1.854−14.324 65.684 1.00 11.36 A ATOM 775 CG LEU A 98 2.512 −15.031 64.4961.00 12.62 A ATOM 776 CD1 LEU A 98 1.679 −14.830 63.227 1.00 12.76 AATOM 777 CD2 LEU A 98 3.921 −14.487 64.305 1.00 12.17 A ATOM 778 C LEU A98 1.763 −13.770 68.111 1.00 11.92 A ATOM 779 O LEU A 98 2.257 −12.69568.460 1.00 12.04 A ATOM 780 N ALA A 99 0.621 −14.237 68.606 1.00 12.12A ATOM 781 CA ALA A 99 −0.144 −13.492 69.602 1.00 12.56 A ATOM 782 CBALA A 99 −1.389 −14.288 70.020 1.00 12.39 A ATOM 783 C ALA A 99 0.695−13.155 70.827 1.00 13.30 A ATOM 784 O ALA A 99 0.474 −12.132 71.4751.00 12.88 A ATOM 785 N MET A 100 1.660 −14.016 71.134 1.00 14.50 A ATOM786 CA MET A 100 2.537 −13.818 72.285 1.00 15.61 A ATOM 787 CB MET A 1002.832 −15.168 72.952 1.00 17.98 A ATOM 788 CG MET A 100 3.608 −15.10574.281 1.00 21.83 A ATOM 789 SD MET A 100 5.365 −14.630 74.196 1.0026.83 A ATOM 790 CE MET A 100 6.114 −16.169 73.669 1.00 24.50 A ATOM 791C MET A 100 3.862 −13.135 71.932 1.00 15.20 A ATOM 792 O MET A 100 4.217−12.113 72.520 1.00 15.12 A ATOM 793 N GLU A 101 4.577 −13.687 70.9581.00 13.89 A ATOM 794 CA GLU A 101 5.890 −13.163 70.586 1.00 13.45 AATOM 795 CB GLU A 101 6.616 −14.187 69.713 1.00 13.61 A ATOM 796 CG GLUA 101 8.094 −13.880 69.475 1.00 13.97 A ATOM 797 CD GLU A 101 8.942−13.936 70.741 1.00 14.80 A ATOM 798 OE1 GLU A 101 8.422 −14.335 71.8081.00 15.03 A ATOM 799 OE2 GLU A 101 10.143 −13.584 70.666 1.00 14.42 AATOM 800 C GLU A 101 5.980 −11.778 69.933 1.00 13.03 A ATOM 801 O GLU A101 6.860 −10.993 70.286 1.00 11.63 A ATOM 802 N VAL A 102 5.097 −11.46968.985 1.00 12.32 A ATOM 803 CA VAL A 102 5.160 −10.161 68.340 1.0012.06 A ATOM 804 CB VAL A 102 4.054 −10.002 67.271 1.00 12.10 A ATOM 805CG1 VAL A 102 4.043 −8.579 66.730 1.00 12.24 A ATOM 806 CG2 VAL A 1024.312 −10.982 66.120 1.00 12.82 A ATOM 807 C VAL A 102 5.071 −9.03569.378 1.00 12.40 A ATOM 808 O VAL A 102 5.911 −8.135 69.388 1.00 12.03A ATOM 809 N PRO A 103 4.061 −9.072 70.268 1.00 12.59 A ATOM 810 CD PROA 103 2.862 −9.928 70.270 1.00 12.42 A ATOM 811 CA PRO A 103 3.942−8.020 71.284 1.00 12.41 A ATOM 812 CB PRO A 103 2.585 −8.312 71.9311.00 13.58 A ATOM 813 CG PRO A 103 1.819 −9.000 70.828 1.00 13.22 A ATOM814 C PRO A 103 5.085 −8.056 72.312 1.00 12.46 A ATOM 815 O PRO A 1035.570 −7.008 72.748 1.00 11.92 A ATOM 816 N ARG A 104 5.512 −9.25672.705 1.00 12.35 A ATOM 817 CA ARG A 104 6.593 −9.376 73.691 1.00 12.83A ATOM 818 CB ARG A 104 6.830 −10.841 74.073 1.00 13.38 A ATOM 819 CGARG A 104 7.824 −11.005 75.233 1.00 14.51 A ATOM 820 CD ARG A 104 8.463−12.393 75.252 1.00 15.96 A ATOM 821 NE ARG A 104 9.362 −12.594 74.1161.00 17.99 A ATOM 822 CZ ARG A 104 10.561 −12.031 73.994 1.00 19.06 AATOM 823 NH1 ARG A 104 11.025 −11.228 74.946 1.00 19.58 A ATOM 824 NH2ARG A 104 11.295 −12.260 72.911 1.00 19.03 A ATOM 825 C ARG A 104 7.907−8.789 73.179 1.00 12.54 A ATOM 826 O ARG A 104 8.559 −8.002 73.867 1.0012.97 A ATOM 827 N LEU A 105 8.297 −9.190 71.972 1.00 12.55 A ATOM 828CA LEU A 105 9.532 −8.722 71.356 1.00 12.96 A ATOM 829 CB LEU A 1059.768 −9.491 70.047 1.00 13.70 A ATOM 830 CG LEU A 105 11.113 −9.41769.327 1.00 15.14 A ATOM 831 CD1 LEU A 105 12.227 −9.949 70.231 1.0014.66 A ATOM 832 CD2 LEU A 105 11.028 −10.247 68.034 1.00 14.82 A ATOM833 C LEU A 105 9.454 −7.219 71.094 1.00 12.85 A ATOM 834 O LEU A 10510.436 −6.494 71.271 1.00 12.86 A ATOM 835 N GLY A 106 8.278 −6.75470.675 1.00 12.06 A ATOM 836 CA GLY A 106 8.086 −5.337 70.412 1.00 11.77A ATOM 837 C GLY A 106 8.215 −4.504 71.675 1.00 11.78 A ATOM 838 O GLY A106 8.767 −3.405 71.648 1.00 11.19 A ATOM 839 N LYS A 107 7.710 −5.02572.790 1.00 11.65 A ATOM 840 CA LYS A 107 7.800 −4.312 74.060 1.00 12.93A ATOM 841 CB LYS A 107 6.993 −5.029 75.145 1.00 14.06 A ATOM 842 CG LYSA 107 6.987 −4.280 76.465 1.00 15.87 A ATOM 843 CD LYS A 107 7.048−5.223 77.649 1.00 17.85 A ATOM 844 CE LYS A 107 7.068 −4.444 78.9541.00 19.08 A ATOM 845 NZ LYS A 107 7.304 −5.335 80.128 1.00 21.55 A ATOM846 C LYS A 107 9.255 −4.203 74.520 1.00 13.01 A ATOM 847 O LYS A 1079.664 −3.180 75.067 1.00 13.04 A ATOM 848 N GLU A 108 10.034 −5.26074.302 1.00 13.42 A ATOM 849 CA GLU A 108 11.441 −5.264 74.702 1.0013.99 A ATOM 850 CB GLU A 108 12.081 −6.618 74.360 1.00 15.13 A ATOM 851CG GLU A 108 13.507 −6.782 74.851 1.00 16.71 A ATOM 852 CD GLU A 10814.044 −8.195 74.660 1.00 17.86 A ATOM 853 OE1 GLU A 108 15.250 −8.40874.910 1.00 18.93 A ATOM 854 OE2 GLU A 108 13.265 −9.088 74.267 1.0016.99 A ATOM 855 C GLU A 108 12.208 −4.122 74.019 1.00 13.77 A ATOM 856O GLU A 108 13.015 −3.433 74.651 1.00 13.37 A ATOM 857 N ALA A 10911.954 −3.922 72.728 1.00 12.99 A ATOM 858 CA ALA A 109 12.618 −2.85571.981 1.00 12.44 A ATOM 859 CB ALA A 109 12.370 −3.027 70.494 1.0011.96 A ATOM 860 C ALA A 109 12.105 −1.491 72.440 1.00 12.31 A ATOM 861O ALA A 109 12.881 −0.543 72.595 1.00 11.79 A ATOM 862 N ALA A 11010.796 −1.400 72.657 1.00 11.92 A ATOM 863 CA ALA A 110 10.170 −0.15473.093 1.00 12.92 A ATOM 864 CB ALA A 110 8.655 −0.335 73.173 1.00 12.53A ATOM 865 C ALA A 110 10.712 0.332 74.440 1.00 13.13 A ATOM 866 O ALA A110 10.938 1.528 74.632 1.00 13.01 A ATOM 867 N VAL A 111 10.923 −0.59275.371 1.00 13.59 A ATOM 868 CA VAL A 111 11.442 −0.219 76.683 1.0014.30 A ATOM 869 CB VAL A 111 11.512 −1.445 77.632 1.00 14.16 A ATOM 870CG1 VAL A 111 12.249 −1.073 78.921 1.00 14.90 A ATOM 871 CG2 VAL A 11110.102 −1.915 77.972 1.00 14.85 A ATOM 872 C VAL A 111 12.830 0.41276.549 1.00 14.57 A ATOM 873 O VAL A 111 13.140 1.393 77.232 1.00 14.48A ATOM 874 N LYS A 112 13.655 −0.140 75.660 1.00 14.33 A ATOM 875 CA LYSA 112 15.003 0.382 75.439 1.00 14.52 A ATOM 876 CB LYS A 112 15.803−0.550 74.522 1.00 15.84 A ATOM 877 CG LYS A 112 16.113 −1.911 75.1181.00 17.43 A ATOM 878 CD LYS A 112 16.934 −2.747 74.147 1.00 18.69 AATOM 879 CE LYS A 112 17.182 −4.137 74.687 1.00 19.96 A ATOM 880 NZ LYSA 112 17.933 −4.976 73.708 1.00 20.59 A ATOM 881 C LYS A 112 14.9731.783 74.829 1.00 14.19 A ATOM 882 O LYS A 112 15.771 2.645 75.198 1.0013.66 A ATOM 883 N ALA A 113 14.054 2.008 73.894 1.00 13.82 A ATOM 884CA ALA A 113 13.935 3.316 73.252 1.00 13.94 A ATOM 885 CB ALA A 11312.985 3.227 72.039 1.00 13.86 A ATOM 886 C ALA A 113 13.443 4.38474.235 1.00 13.81 A ATOM 887 O ALA A 113 13.923 5.519 74.228 1.00 13.80A ATOM 888 N ILE A 114 12.492 4.014 75.085 1.00 13.62 A ATOM 889 CA ILEA 114 11.939 4.938 76.067 1.00 14.81 A ATOM 890 CB ILE A 114 10.6904.325 76.751 1.00 14.96 A ATOM 891 CG2 ILE A 114 10.205 5.229 77.8741.00 15.35 A ATOM 892 CG1 ILE A 114 9.592 4.106 75.702 1.00 15.11 A ATOM893 CD1 ILE A 114 8.359 3.358 76.211 1.00 14.83 A ATOM 894 C ILE A 11412.993 5.301 77.118 1.00 15.14 A ATOM 895 O ILE A 114 13.031 6.43077.607 1.00 14.81 A ATOM 896 N LYS A 115 13.851 4.341 77.452 1.00 15.95A ATOM 897 CA LYS A 115 14.915 4.572 78.427 1.00 17.10 A ATOM 898 CB LYSA 115 15.664 3.264 78.723 1.00 18.03 A ATOM 899 CG LYS A 115 16.7933.422 79.732 1.00 20.46 A ATOM 900 CD LYS A 115 17.665 2.176 79.815 1.0022.06 A ATOM 901 CE LYS A 115 18.867 2.413 80.730 1.00 24.19 A ATOM 902NZ LYS A 115 19.768 1.230 80.814 1.00 24.53 A ATOM 903 C LYS A 11515.896 5.615 77.882 1.00 16.58 A ATOM 904 O LYS A 115 16.293 6.53678.596 1.00 16.08 A ATOM 905 N GLU A 116 16.282 5.470 76.615 1.00 15.74A ATOM 906 CA GLU A 116 17.209 6.413 75.989 1.00 15.99 A ATOM 907 CB GLUA 116 17.559 5.973 74.563 1.00 15.39 A ATOM 908 CG GLU A 116 18.6066.860 73.895 1.00 16.97 A ATOM 909 CD GLU A 116 18.736 6.634 72.392 1.0017.20 A ATOM 910 OE1 GLU A 116 18.375 5.542 71.907 1.00 16.77 A ATOM 911OE2 GLU A 116 19.219 7.553 71.694 1.00 17.90 A ATOM 912 C GLU A 11616.576 7.807 75.935 1.00 16.26 A ATOM 913 O GLU A 116 17.223 8.81176.250 1.00 15.55 A ATOM 914 N TRP A 117 15.312 7.853 75.520 1.00 16.06A ATOM 915 CA TRP A 117 14.561 9.102 75.424 1.00 16.63 A ATOM 916 CB TRPA 117 13.113 8.792 75.026 1.00 15.45 A ATOM 917 CG TRP A 117 12.2229.992 74.851 1.00 15.18 A ATOM 918 CD2 TRP A 117 10.815 10.061 75.1301.00 14.59 A ATOM 919 CE2 TRP A 117 10.372 11.344 74.735 1.00 14.57 AATOM 920 CE3 TRP A 117 9.885 9.162 75.672 1.00 14.93 A ATOM 921 CD1 TRPA 117 12.565 11.204 74.320 1.00 14.39 A ATOM 922 NE1 TRP A 117 11.45912.019 74.246 1.00 14.28 A ATOM 923 CZ2 TRP A 117 9.038 11.752 74.8641.00 14.45 A ATOM 924 CZ3 TRP A 117 8.555 9.569 75.801 1.00 14.58 A ATOM925 CH2 TRP A 117 8.147 10.852 75.397 1.00 14.55 A ATOM 926 C TRP A 11714.615 9.836 76.765 1.00 17.46 A ATOM 927 O TRP A 117 14.919 11.02676.812 1.00 17.93 A ATOM 928 N GLY A 118 14.322 9.120 77.848 1.00 18.47A ATOM 929 CA GLY A 118 14.375 9.713 79.175 1.00 19.45 A ATOM 930 C GLYA 118 13.121 10.377 79.724 1.00 20.29 A ATOM 931 O GLY A 118 13.11010.800 80.883 1.00 20.22 A ATOM 932 N GLN A 119 12.066 10.469 78.9181.00 20.22 A ATOM 933 CA GLN A 119 10.825 11.100 79.363 1.00 20.78 AATOM 934 CB GLN A 119 10.282 12.014 78.257 1.00 21.39 A ATOM 935 CG GLNA 119 11.219 13.173 77.913 1.00 23.09 A ATOM 936 CD GLN A 119 11.65513.958 79.146 1.00 23.77 A ATOM 937 OE1 GLN A 119 10.824 14.468 79.8991.00 24.98 A ATOM 938 NE2 GLN A 119 12.962 14.050 79.357 1.00 24.40 AATOM 939 C GLN A 119 9.763 10.079 79.782 1.00 20.88 A ATOM 940 O GLN A119 9.859 8.903 79.443 1.00 20.86 A ATOM 941 N PRO A 120 8.733 10.52480.525 1.00 21.16 A ATOM 942 CD PRO A 120 8.517 11.921 80.939 1.00 21.29A ATOM 943 CA PRO A 120 7.641 9.667 81.008 1.00 21.57 A ATOM 944 CB PROA 120 6.746 10.643 81.772 1.00 21.80 A ATOM 945 CG PRO A 120 7.67711.753 82.165 1.00 22.42 A ATOM 946 C PRO A 120 6.877 8.983 79.873 1.0021.27 A ATOM 947 O PRO A 120 6.608 9.607 78.851 1.00 21.61 A ATOM 948 NLYS A 121 6.519 7.714 80.056 1.00 21.35 A ATOM 949 CA LYS A 121 5.7776.977 79.029 1.00 21.42 A ATOM 950 CB LYS A 121 5.623 5.501 79.421 1.0022.56 A ATOM 951 CG LYS A 121 4.759 5.288 80.654 1.00 25.13 A ATOM 952CD LYS A 121 4.399 3.822 80.900 1.00 26.18 A ATOM 953 CE LYS A 121 5.6192.984 81.222 1.00 27.36 A ATOM 954 NZ LYS A 121 5.225 1.655 81.786 1.0028.12 A ATOM 955 C LYS A 121 4.392 7.595 78.840 1.00 20.94 A ATOM 956 OLYS A 121 3.762 7.429 77.791 1.00 20.02 A ATOM 957 N SER A 122 3.9288.309 79.863 1.00 19.98 A ATOM 958 CA SER A 122 2.621 8.956 79.836 1.0019.81 A ATOM 959 CB SER A 122 2.252 9.457 81.236 1.00 20.86 A ATOM 960OG SER A 122 3.131 10.488 81.656 1.00 20.86 A ATOM 961 C SER A 122 2.58010.121 78.856 1.00 19.21 A ATOM 962 O SER A 122 1.508 10.633 78.533 1.0019.72 A ATOM 963 N LYS A 123 3.748 10.540 78.380 1.00 18.76 A ATOM 964CA LYS A 123 3.819 11.646 77.435 1.00 17.51 A ATOM 965 CB LYS A 1235.069 12.486 77.715 1.00 19.70 A ATOM 966 CG LYS A 123 5.096 13.00479.157 1.00 21.88 A ATOM 967 CD LYS A 123 6.289 13.894 79.465 1.00 24.26A ATOM 968 CE LYS A 123 6.204 15.233 78.751 1.00 25.53 A ATOM 969 NZ LYSA 123 7.195 16.202 79.318 1.00 26.85 A ATOM 970 C LYS A 123 3.782 11.17975.975 1.00 16.02 A ATOM 971 O LYS A 123 3.874 11.990 75.056 1.00 15.29A ATOM 972 N ILE A 124 3.649 9.871 75.767 1.00 14.24 A ATOM 973 CA ILE A124 3.551 9.326 74.413 1.00 13.14 A ATOM 974 CB ILE A 124 3.949 7.82874.370 1.00 13.63 A ATOM 975 CG2 ILE A 124 3.612 7.235 73.000 1.00 13.42A ATOM 976 CG1 ILE A 124 5.451 7.685 74.668 1.00 13.73 A ATOM 977 CD1ILE A 124 5.932 6.250 74.850 1.00 14.46 A ATOM 978 C ILE A 124 2.0849.503 74.016 1.00 12.41 A ATOM 979 O ILE A 124 1.184 9.010 74.695 1.0012.34 A ATOM 980 N THR A 125 1.853 10.219 72.922 1.00 11.64 A ATOM 981CA THR A 125 0.499 10.515 72.451 1.00 10.75 A ATOM 982 CB THR A 1250.409 11.975 71.989 1.00 9.91 A ATOM 983 OG1 THR A 125 1.357 12.19670.937 1.00 10.98 A ATOM 984 CG2 THR A 125 0.714 12.921 73.147 1.0010.30 A ATOM 985 C THR A 125 −0.030 9.639 71.313 1.00 10.65 A ATOM 986 OTHR A 125 −1.249 9.502 71.150 1.00 10.36 A ATOM 987 N HIS A 126 0.8779.078 70.516 1.00 10.15 A ATOM 988 CA HIS A 126 0.494 8.223 69.389 1.009.76 A ATOM 989 CB HIS A 126 0.735 8.936 68.047 1.00 9.29 A ATOM 990 CGHIS A 126 −0.054 10.195 67.858 1.00 9.51 A ATOM 991 CD2 HIS A 126 −1.04710.498 66.987 1.00 10.73 A ATOM 992 ND1 HIS A 126 0.185 11.346 68.5801.00 9.94 A ATOM 993 CE1 HIS A 126 −0.624 12.303 68.159 1.00 10.59 AATOM 994 NE2 HIS A 126 −1.381 11.815 67.193 1.00 10.64 A ATOM 995 C HISA 126 1.329 6.935 69.390 1.00 9.52 A ATOM 996 O HIS A 126 2.463 6.92669.870 1.00 9.39 A ATOM 997 N LEU A 127 0.770 5.865 68.826 1.00 8.68 AATOM 998 CA LEU A 127 1.457 4.577 68.741 1.00 8.66 A ATOM 999 CB LEU A127 0.943 3.615 69.820 1.00 8.64 A ATOM 1000 CG LEU A 127 1.448 2.16769.722 1.00 9.47 A ATOM 1001 CD1 LEU A 127 2.954 2.119 69.949 1.00 9.18A ATOM 1002 CD2 LEU A 127 0.728 1.298 70.748 1.00 9.28 A ATOM 1003 C LEUA 127 1.243 3.927 67.379 1.00 8.85 A ATOM 1004 O LEU A 127 0.107 3.73766.956 1.00 7.92 A ATOM 1005 N ILE A 128 2.339 3.580 66.710 1.00 8.63 AATOM 1006 CA ILE A 128 2.280 2.921 65.407 1.00 8.91 A ATOM 1007 CB ILE A128 3.054 3.717 64.324 1.00 8.76 A ATOM 1008 CG2 ILE A 128 3.053 2.94263.007 1.00 9.37 A ATOM 1009 CG1 ILE A 128 2.436 5.110 64.144 1.00 8.68A ATOM 1010 CD1 ILE A 128 3.161 5.984 63.137 1.00 8.20 A ATOM 1011 C ILEA 128 2.950 1.551 65.541 1.00 9.26 A ATOM 1012 O ILE A 128 4.142 1.47765.847 1.00 9.52 A ATOM 1013 N VAL A 129 2.195 0.475 65.329 1.00 9.33 AATOM 1014 CA VAL A 129 2.768 −0.872 65.408 1.00 9.83 A ATOM 1015 CB VALA 129 2.095 −1.728 66.500 1.00 9.91 A ATOM 1016 CG1 VAL A 129 2.655−3.151 66.465 1.00 9.78 A ATOM 1017 CG2 VAL A 129 2.342 −1.099 67.8731.00 8.95 A ATOM 1018 C VAL A 129 2.621 −1.571 64.063 1.00 10.19 A ATOM1019 O VAL A 129 1.524 −1.638 63.504 1.00 10.94 A ATOM 1020 N CYS A 1303.739 −2.089 63.561 1.00 10.12 A ATOM 1021 CA CYS A 130 3.803 −2.76562.268 1.00 10.10 A ATOM 1022 CB CYS A 130 4.696 −1.946 61.328 1.0010.57 A ATOM 1023 SG CYS A 130 5.174 −2.737 59.758 1.00 12.03 A ATOM1024 C CYS A 130 4.343 −4.194 62.363 1.00 9.44 A ATOM 1025 O CYS A 1305.309 −4.455 63.078 1.00 9.20 A ATOM 1026 N SER A 131 3.702 −5.10961.641 1.00 8.71 A ATOM 1027 CA SER A 131 4.117 −6.516 61.579 1.00 9.13A ATOM 1028 CB SER A 131 3.590 −7.297 62.788 1.00 9.14 A ATOM 1029 OGSER A 131 4.170 −8.592 62.834 1.00 8.81 A ATOM 1030 C SER A 131 3.535−7.098 60.293 1.00 9.18 A ATOM 1031 O SER A 131 2.451 −6.699 59.878 1.009.08 A ATOM 1032 N THR A 132 4.246 −8.028 59.655 1.00 10.48 A ATOM 1033CA THR A 132 3.754 −8.620 58.411 1.00 10.93 A ATOM 1034 CB THR A 1324.689 −9.774 57.941 1.00 11.08 A ATOM 1035 OG1 THR A 132 5.988 −9.23257.654 1.00 10.58 A ATOM 1036 CG2 THR A 132 4.150 −10.437 56.675 1.0011.82 A ATOM 1037 C THR A 132 2.294 −9.089 58.544 1.00 11.41 A ATOM 1038O THR A 132 1.505 −8.928 57.607 1.00 11.93 A ATOM 1039 N THR A 133 1.928−9.647 59.701 1.00 11.44 A ATOM 1040 CA THR A 133 0.541 −10.075 59.9601.00 11.06 A ATOM 1041 CB THR A 133 0.301 −11.586 59.681 1.00 12.44 AATOM 1042 OG1 THR A 133 0.982 −12.371 60.675 1.00 12.81 A ATOM 1043 CG2THR A 133 0.798 −11.975 58.292 1.00 12.09 A ATOM 1044 C THR A 133 0.171−9.867 61.432 1.00 11.34 A ATOM 1045 O THR A 133 1.038 −9.591 62.2621.00 10.26 A ATOM 1046 N THR A 134 −1.121 −9.972 61.741 1.00 10.39 AATOM 1047 CA THR A 134 −1.599 −9.886 63.127 1.00 10.86 A ATOM 1048 CBTHR A 134 −2.151 −8.478 63.490 1.00 10.72 A ATOM 1049 OG1 THR A 134−2.068 −8.297 64.913 1.00 10.97 A ATOM 1050 CG2 THR A 134 −3.595 −8.31063.049 1.00 9.79 A ATOM 1051 C THR A 134 −2.681 −10.973 63.214 1.0010.76 A ATOM 1052 O THR A 134 −3.493 −11.124 62.307 1.00 10.88 A ATOM1053 N PRO A 135 −2.696 −11.753 64.305 1.00 10.68 A ATOM 1054 CD PRO A135 −1.766 −11.689 65.450 1.00 10.93 A ATOM 1055 CA PRO A 135 −3.665−12.840 64.483 1.00 11.06 A ATOM 1056 CB PRO A 135 −2.969 −13.736 65.5021.00 10.76 A ATOM 1057 CG PRO A 135 −2.338 −12.722 66.415 1.00 10.45 AATOM 1058 C PRO A 135 −5.105 −12.568 64.890 1.00 11.42 A ATOM 1059 O PROA 135 −5.999 −13.341 64.538 1.00 11.28 A ATOM 1060 N ASP A 136 −5.352−11.481 65.608 1.00 11.37 A ATOM 1061 CA ASP A 136 −6.704 −11.235 66.0911.00 12.18 A ATOM 1062 CB ASP A 136 −6.774 −11.593 67.587 1.00 13.43 AATOM 1063 CG ASP A 136 −6.122 −12.935 67.916 1.00 14.45 A ATOM 1064 OD1ASP A 136 −5.193 −12.973 68.762 1.00 13.87 A ATOM 1065 OD2 ASP A 136−6.544 −13.955 67.343 1.00 14.97 A ATOM 1066 C ASP A 136 −7.199 −9.80265.942 1.00 12.49 A ATOM 1067 O ASP A 136 −6.625 −8.983 65.225 1.0012.60 A ATOM 1068 N LEU A 137 −8.310 −9.546 66.627 1.00 12.88 A ATOM1069 CA LEU A 137 −8.924 −8.230 66.740 1.00 13.15 A ATOM 1070 CB LEU A137 −10.244 −8.126 65.967 1.00 13.24 A ATOM 1071 CG LEU A 137 −10.145−7.967 64.450 1.00 13.68 A ATOM 1072 CD1 LEU A 137 −10.283 −9.326 63.7981.00 14.40 A ATOM 1073 CD2 LEU A 137 −11.235 −7.023 63.957 1.00 14.51 AATOM 1074 C LEU A 137 −9.212 −8.202 68.231 1.00 13.21 A ATOM 1075 O LEUA 137 −9.906 −9.080 68.741 1.00 13.93 A ATOM 1076 N PRO A 138 −8.660−7.225 68.963 1.00 13.99 A ATOM 1077 CD PRO A 138 −8.996 −7.174 70.3961.00 14.42 A ATOM 1078 CA PRO A 138 −7.780 −6.107 68.602 1.00 13.83 AATOM 1079 CB PRO A 138 −7.565 −5.401 69.941 1.00 14.52 A ATOM 1080 CGPRO A 138 −8.802 −5.728 70.705 1.00 14.81 A ATOM 1081 C PRO A 138 −6.444−6.511 67.956 1.00 14.18 A ATOM 1082 O PRO A 138 −5.955 −7.621 68.1661.00 13.48 A ATOM 1083 N GLY A 139 −5.872 −5.598 67.170 1.00 13.47 AATOM 1084 CA GLY A 139 −4.596 −5.841 66.515 1.00 13.68 A ATOM 1085 C GLYA 139 −3.441 −5.742 67.504 1.00 13.10 A ATOM 1086 O GLY A 139 −3.664−5.427 68.668 1.00 13.23 A ATOM 1087 N ALA A 140 −2.212 −5.995 67.0561.00 12.38 A ATOM 1088 CA ALA A 140 −1.056 −5.938 67.961 1.00 12.40 AATOM 1089 CB ALA A 140 0.216 −6.393 67.236 1.00 10.91 A ATOM 1090 C ALAA 140 −0.823 −4.568 68.611 1.00 12.51 A ATOM 1091 O ALA A 140 −0.152−4.483 69.643 1.00 12.15 A ATOM 1092 N ASP A 141 −1.359 −3.499 68.0241.00 12.33 A ATOM 1093 CA ASP A 141 −1.191 −2.173 68.622 1.00 12.63 AATOM 1094 CB ASP A 141 −1.785 −1.081 67.724 1.00 13.06 A ATOM 1095 CGASP A 141 −3.207 −1.384 67.287 1.00 13.39 A ATOM 1096 OD1 ASP A 141−3.413 −2.385 66.564 1.00 13.50 A ATOM 1097 OD2 ASP A 141 −4.119 −0.61867.661 1.00 13.61 A ATOM 1098 C ASP A 141 −1.856 −2.140 70.000 1.0012.86 A ATOM 1099 O ASP A 141 −1.319 −1.562 70.948 1.00 12.35 A ATOM1100 N TYR A 142 −3.022 −2.774 70.110 1.00 13.35 A ATOM 1101 CA TYR A142 −3.747 −2.836 71.377 1.00 13.60 A ATOM 1102 CB TYR A 142 −5.090−3.549 71.182 1.00 14.21 A ATOM 1103 CG TYR A 142 −5.781 −3.900 72.4781.00 15.51 A ATOM 1104 CD1 TYR A 142 −6.503 −2.943 73.193 1.00 15.93 AATOM 1105 CE1 TYR A 142 −7.110 −3.262 74.411 1.00 17.60 A ATOM 1106 CD2TYR A 142 −5.680 −5.184 73.012 1.00 16.59 A ATOM 1107 CE2 TYR A 142−6.275 −5.509 74.224 1.00 17.58 A ATOM 1108 CZ TYR A 142 −6.988 −4.54974.917 1.00 18.62 A ATOM 1109 OH TYR A 142 −7.587 −4.890 76.112 1.0020.44 A ATOM 1110 C TYR A 142 −2.932 −3.584 72.441 1.00 13.98 A ATOM1111 O TYR A 142 −2.773 −3.109 73.572 1.00 13.20 A ATOM 1112 N GLN A 143−2.420 −4.757 72.080 1.00 14.49 A ATOM 1113 CA GLN A 143 −1.635 −5.55173.023 1.00 15.02 A ATOM 1114 CB GLN A 143 −1.239 −6.896 72.403 1.0016.02 A ATOM 1115 CG GLN A 143 −2.406 −7.861 72.183 1.00 17.48 A ATOM1116 CD GLN A 143 −3.193 −8.148 73.455 1.00 18.91 A ATOM 1117 OE1 GLN A143 −2.621 −8.294 74.539 1.00 18.85 A ATOM 1118 NE2 GLN A 143 −4.515−8.246 73.324 1.00 20.56 A ATOM 1119 C GLN A 143 −0.385 −4.824 73.5181.00 15.31 A ATOM 1120 O GLN A 143 −0.047 −4.908 74.703 1.00 15.22 AATOM 1121 N LEU A 144 0.303 −4.113 72.626 1.00 14.97 A ATOM 1122 CA LEUA 144 1.506 −3.385 73.032 1.00 15.35 A ATOM 1123 CB LEU A 144 2.189−2.716 71.832 1.00 16.16 A ATOM 1124 CG LEU A 144 3.669 −3.050 71.6001.00 17.50 A ATOM 1125 CD1 LEU A 144 4.321 −1.918 70.822 1.00 18.53 AATOM 1126 CD2 LEU A 144 4.399 −3.242 72.926 1.00 18.13 A ATOM 1127 C LEUA 144 1.150 −2.317 74.061 1.00 15.11 A ATOM 1128 O LEU A 144 1.880−2.110 75.030 1.00 14.55 A ATOM 1129 N THR A 145 0.030 −1.635 73.8381.00 14.64 A ATOM 1130 CA THR A 145 −0.442 −0.599 74.752 1.00 15.04 AATOM 1131 CB THR A 145 −1.769 0.018 74.258 1.00 15.52 A ATOM 1132 OG1THR A 145 −1.544 0.707 73.023 1.00 15.30 A ATOM 1133 CG2 THR A 145−2.325 0.993 75.288 1.00 15.63 A ATOM 1134 C THR A 145 −0.678 −1.21576.130 1.00 15.20 A ATOM 1135 O THR A 145 −0.310 −0.640 77.156 1.0014.90 A ATOM 1136 N LYS A 146 −1.296 −2.392 76.138 1.00 15.71 A ATOM1137 CA LYS A 146 −1.587 −3.116 77.374 1.00 16.56 A ATOM 1138 CB LYS A146 −2.469 −4.325 77.054 1.00 17.61 A ATOM 1139 CG LYS A 146 −2.785−5.242 78.232 1.00 19.39 A ATOM 1140 CD LYS A 146 −3.567 −6.463 77.7451.00 21.39 A ATOM 1141 CE LYS A 146 −3.488 −7.618 78.725 1.00 22.15 AATOM 1142 NZ LYS A 146 −4.011 −8.877 78.116 1.00 23.90 A ATOM 1143 C LYSA 146 −0.302 −3.569 78.083 1.00 16.40 A ATOM 1144 O LYS A 146 −0.176−3.421 79.302 1.00 16.41 A ATOM 1145 N LEU A 147 0.654 −4.102 77.3221.00 16.28 A ATOM 1146 CA LEU A 147 1.912 −4.579 77.901 1.00 16.03 AATOM 1147 CB LEU A 147 2.717 −5.387 76.872 1.00 16.79 A ATOM 1148 CG LEUA 147 2.089 −6.628 76.224 1.00 17.91 A ATOM 1149 CD1 LEU A 147 3.145−7.359 75.409 1.00 18.58 A ATOM 1150 CD2 LEU A 147 1.520 −7.551 77.2771.00 19.05 A ATOM 1151 C LEU A 147 2.789 −3.449 78.446 1.00 15.74 A ATOM1152 O LEU A 147 3.477 −3.622 79.456 1.00 15.01 A ATOM 1153 N LEU A 1482.765 −2.297 77.780 1.00 14.59 A ATOM 1154 CA LEU A 148 3.567 −1.14978.202 1.00 14.85 A ATOM 1155 CB LEU A 148 3.913 −0.261 76.998 1.0014.25 A ATOM 1156 CG LEU A 148 4.991 −0.710 76.017 1.00 14.59 A ATOM1157 CD1 LEU A 148 4.989 0.201 74.790 1.00 14.37 A ATOM 1158 CD2 LEU A148 6.349 −0.680 76.712 1.00 15.53 A ATOM 1159 C LEU A 148 2.877 −0.28979.257 1.00 14.60 A ATOM 1160 O LEU A 148 3.535 0.459 79.981 1.00 14.89A ATOM 1161 N GLY A 149 1.554 −0.381 79.336 1.00 14.31 A ATOM 1162 CAGLY A 149 0.822 0.426 80.295 1.00 14.76 A ATOM 1163 C GLY A 149 0.7541.885 79.867 1.00 15.29 A ATOM 1164 O GLY A 149 0.838 2.792 80.696 1.0015.01 A ATOM 1165 N LEU A 150 0.618 2.123 78.565 1.00 15.01 A ATOM 1166CA LEU A 150 0.522 3.490 78.058 1.00 14.43 A ATOM 1167 CB LEU A 1500.665 3.500 76.530 1.00 14.29 A ATOM 1168 CG LEU A 150 1.962 2.94075.928 1.00 14.95 A ATOM 1169 CD1 LEU A 150 1.852 2.932 74.401 1.0015.08 A ATOM 1170 CD2 LEU A 150 3.157 3.773 76.374 1.00 14.06 A ATOM1171 C LEU A 150 −0.851 4.041 78.451 1.00 14.48 A ATOM 1172 O LEU A 150−1.729 3.278 78.853 1.00 14.49 A ATOM 1173 N ARG A 151 −1.043 5.35678.348 1.00 14.75 A ATOM 1174 CA ARG A 151 −2.343 5.942 78.686 1.0015.18 A ATOM 1175 CB ARG A 151 −2.363 7.447 78.418 1.00 16.74 A ATOM1176 CG ARG A 151 −1.317 8.281 79.141 1.00 20.10 A ATOM 1177 CD ARG A151 −1.614 8.453 80.619 1.00 22.50 A ATOM 1178 NE ARG A 151 −1.242 7.28581.409 1.00 25.48 A ATOM 1179 CZ ARG A 151 −0.889 7.345 82.690 1.0026.63 A ATOM 1180 NH1 ARG A 151 −0.863 8.517 83.315 1.00 27.54 A ATOM1181 NH2 ARG A 151 −0.554 6.240 83.345 1.00 27.39 A ATOM 1182 C ARG A151 −3.376 5.285 77.767 1.00 14.81 A ATOM 1183 O ARG A 151 −3.086 5.01776.597 1.00 14.19 A ATOM 1184 N PRO A 152 −4.594 5.026 78.276 1.00 14.13A ATOM 1185 CD PRO A 152 −5.080 5.236 79.652 1.00 14.92 A ATOM 1186 CAPRO A 152 −5.626 4.397 77.440 1.00 13.82 A ATOM 1187 CB PRO A 152 −6.7684.139 78.427 1.00 14.60 A ATOM 1188 CG PRO A 152 −6.581 5.212 79.4691.00 15.28 A ATOM 1189 C PRO A 152 −6.063 5.243 76.244 1.00 13.54 A ATOM1190 O PRO A 152 −6.637 4.718 75.285 1.00 13.02 A ATOM 1191 N TYR A 153−5.782 6.543 76.296 1.00 12.81 A ATOM 1192 CA TYR A 153 −6.160 7.44775.215 1.00 12.98 A ATOM 1193 CB TYR A 153 −6.697 8.760 75.799 1.0013.85 A ATOM 1194 CG TYR A 153 −5.834 9.362 76.879 1.00 15.46 A ATOM1195 CD1 TYR A 153 −4.728 10.150 76.559 1.00 15.67 A ATOM 1196 CE1 TYR A153 −3.933 10.713 77.558 1.00 16.87 A ATOM 1197 CD2 TYR A 153 −6.1249.145 78.228 1.00 15.87 A ATOM 1198 CE2 TYR A 153 −5.335 9.700 79.2331.00 16.78 A ATOM 1199 CZ TYR A 153 −4.243 10.484 78.892 1.00 16.94 AATOM 1200 OH TYR A 153 −3.466 11.045 79.887 1.00 18.20 A ATOM 1201 C TYRA 153 −5.046 7.714 74.198 1.00 12.40 A ATOM 1202 O TYR A 153 −5.0728.707 73.471 1.00 11.41 A ATOM 1203 N VAL A 154 −4.061 6.822 74.157 1.0011.87 A ATOM 1204 CA VAL A 154 −2.980 6.940 73.185 1.00 11.77 A ATOM1205 CB VAL A 154 −1.853 5.908 73.489 1.00 11.94 A ATOM 1206 CG1 VAL A154 −2.405 4.491 73.415 1.00 11.75 A ATOM 1207 CG2 VAL A 154 −0.6896.092 72.525 1.00 11.07 A ATOM 1208 C VAL A 154 −3.648 6.625 71.837 1.0011.61 A ATOM 1209 O VAL A 154 −4.427 5.677 71.746 1.00 11.48 A ATOM 1210N LYS A 155 −3.372 7.434 70.815 1.00 11.04 A ATOM 1211 CA LYS A 155−3.958 7.240 69.488 1.00 11.52 A ATOM 1212 CB LYS A 155 −4.021 8.57968.744 1.00 12.00 A ATOM 1213 CG LYS A 155 −5.109 9.511 69.281 1.0013.78 A ATOM 1214 CD LYS A 155 −5.049 10.889 68.638 1.00 14.84 A ATOM1215 CE LYS A 155 −4.098 11.811 69.373 1.00 16.12 A ATOM 1216 NZ LYS A155 −4.651 12.234 70.700 1.00 17.06 A ATOM 1217 C LYS A 155 −3.144 6.21968.705 1.00 10.94 A ATOM 1218 O LYS A 155 −1.993 6.472 68.349 1.00 10.07A ATOM 1219 N ARG A 156 −3.771 5.077 68.422 1.00 10.42 A ATOM 1220 CAARG A 156 −3.118 3.956 67.748 1.00 10.30 A ATOM 1221 CB ARG A 156 −3.4632.660 68.492 1.00 10.46 A ATOM 1222 CG ARG A 156 −3.114 2.635 69.9841.00 12.15 A ATOM 1223 CD ARG A 156 −3.773 1.430 70.673 1.00 11.65 AATOM 1224 NE ARG A 156 −5.153 1.718 71.061 1.00 13.59 A ATOM 1225 CZ ARGA 156 −6.222 1.026 70.670 1.00 13.73 A ATOM 1226 NH1 ARG A 156 −6.092−0.017 69.860 1.00 13.14 A ATOM 1227 NH2 ARG A 156 −7.429 1.377 71.1011.00 12.93 A ATOM 1228 C ARG A 156 −3.435 3.718 66.271 1.00 10.47 A ATOM1229 O ARG A 156 −4.520 4.034 65.794 1.00 10.65 A ATOM 1230 N VAL A 157−2.470 3.128 65.569 1.00 10.08 A ATOM 1231 CA VAL A 157 −2.629 2.74264.166 1.00 10.38 A ATOM 1232 CB VAL A 157 −2.160 3.834 63.181 1.0010.90 A ATOM 1233 CG1 VAL A 157 −0.714 4.156 63.410 1.00 13.08 A ATOM1234 CG2 VAL A 157 −2.374 3.352 61.739 1.00 12.71 A ATOM 1235 C VAL A157 −1.793 1.484 63.939 1.00 9.54 A ATOM 1236 O VAL A 157 −0.603 1.45664.257 1.00 8.67 A ATOM 1237 N GLY A 158 −2.431 0.440 63.414 1.00 8.62 AATOM 1238 CA GLY A 158 −1.725 −0.801 63.145 1.00 8.95 A ATOM 1239 C GLYA 158 −1.474 −0.920 61.655 1.00 9.11 A ATOM 1240 O GLY A 158 −2.377−0.660 60.861 1.00 9.18 A ATOM 1241 N VAL A 159 −0.252 −1.297 61.2801.00 8.82 A ATOM 1242 CA VAL A 159 0.139 −1.446 59.876 1.00 9.27 A ATOM1243 CB VAL A 159 1.383 −0.578 59.566 1.00 10.03 A ATOM 1244 CG1 VAL A159 1.821 −0.763 58.120 1.00 9.90 A ATOM 1245 CG2 VAL A 159 1.060 0.89059.848 1.00 8.75 A ATOM 1246 C VAL A 159 0.449 −2.918 59.622 1.00 9.42 AATOM 1247 O VAL A 159 1.541 −3.403 59.937 1.00 8.94 A ATOM 1248 N PHE A160 −0.523 −3.620 59.048 1.00 9.07 A ATOM 1249 CA PHE A 160 −0.401−5.049 58.793 1.00 9.95 A ATOM 1250 CB PHE A 160 −1.476 −5.787 59.6071.00 9.65 A ATOM 1251 CG PHE A 160 −1.534 −5.354 61.057 1.00 10.47 AATOM 1252 CD1 PHE A 160 −0.428 −5.519 61.889 1.00 10.51 A ATOM 1253 CD2PHE A 160 −2.679 −4.757 61.577 1.00 10.31 A ATOM 1254 CE1 PHE A 160−0.462 −5.091 63.226 1.00 10.88 A ATOM 1255 CE2 PHE A 160 −2.726 −4.32562.913 1.00 11.26 A ATOM 1256 CZ PHE A 160 −1.618 −4.491 63.735 1.0010.62 A ATOM 1257 C PHE A 160 −0.506 −5.439 57.320 1.00 10.38 A ATOM1258 O PHE A 160 −1.192 −4.787 56.530 1.00 10.36 A ATOM 1259 N GLN A 1610.179 −6.527 56.981 1.00 10.62 A ATOM 1260 CA GLN A 161 0.230 −7.07655.634 1.00 11.79 A ATOM 1261 CB GLN A 161 −1.117 −7.743 55.272 1.0011.33 A ATOM 1262 CG GLN A 161 −1.311 −9.055 56.058 1.00 12.18 A ATOM1263 CD GLN A 161 −2.598 −9.818 55.754 1.00 12.20 A ATOM 1264 OE1 GLN A161 −3.381 −10.113 56.662 1.00 11.95 A ATOM 1265 NE2 GLN A 161 −2.810−10.161 54.487 1.00 12.09 A ATOM 1266 C GLN A 161 0.704 −6.102 54.5541.00 12.04 A ATOM 1267 O GLN A 161 0.215 −6.114 53.421 1.00 13.06 A ATOM1268 N HIS A 162 1.667 −5.256 54.922 1.00 11.82 A ATOM 1269 CA HIS A 1622.279 −4.330 53.975 1.00 12.08 A ATOM 1270 CB HIS A 162 2.552 −2.96254.619 1.00 11.69 A ATOM 1271 CG HIS A 162 1.307 −2.154 54.852 1.0010.82 A ATOM 1272 CD2 HIS A 162 0.161 −2.456 55.507 1.00 9.91 A ATOM1273 ND1 HIS A 162 1.142 −0.874 54.366 1.00 12.15 A ATOM 1274 CE1 HIS A162 −0.051 −0.422 54.711 1.00 9.94 A ATOM 1275 NE2 HIS A 162 −0.667−1.363 55.405 1.00 11.67 A ATOM 1276 C HIS A 162 3.575 −5.021 53.5391.00 12.51 A ATOM 1277 O HIS A 162 3.854 −5.127 52.348 1.00 14.03 A ATOM1278 N GLY A 163 4.361 −5.507 54.497 1.00 12.09 A ATOM 1279 CA GLY A 1635.570 −6.229 54.130 1.00 12.81 A ATOM 1280 C GLY A 163 6.937 −5.60254.325 1.00 12.93 A ATOM 1281 O GLY A 163 7.122 −4.713 55.159 1.00 13.11A ATOM 1282 N CYS A 164 7.898 −6.079 53.533 1.00 12.87 A ATOM 1283 CACYS A 164 9.285 −5.630 53.608 1.00 12.88 A ATOM 1284 CB CYS A 164 10.145−6.435 52.621 1.00 14.32 A ATOM 1285 SG CYS A 164 10.567 −8.126 53.1711.00 18.21 A ATOM 1286 C CYS A 164 9.565 −4.137 53.419 1.00 12.07 A ATOM1287 O CYS A 164 10.611 −3.655 53.851 1.00 12.09 A ATOM 1288 N PHE A 1658.656 −3.402 52.787 1.00 11.32 A ATOM 1289 CA PHE A 165 8.881 −1.97052.579 1.00 11.97 A ATOM 1290 CB PHE A 165 8.268 −1.529 51.239 1.0012.38 A ATOM 1291 CG PHE A 165 6.761 −1.608 51.194 1.00 12.73 A ATOM1292 CD1 PHE A 165 5.977 −0.679 51.878 1.00 12.91 A ATOM 1293 CD2 PHE A165 6.126 −2.624 50.487 1.00 12.52 A ATOM 1294 CE1 PHE A 165 4.582−0.763 51.865 1.00 12.61 A ATOM 1295 CE2 PHE A 165 4.727 −2.719 50.4661.00 12.91 A ATOM 1296 CZ PHE A 165 3.955 −1.785 51.160 1.00 12.54 AATOM 1297 C PHE A 165 8.327 −1.090 53.711 1.00 11.55 A ATOM 1298 O PHE A165 8.591 0.116 53.755 1.00 10.90 A ATOM 1299 N ALA A 166 7.597 −1.70554.640 1.00 11.47 A ATOM 1300 CA ALA A 166 6.951 −0.987 55.742 1.0010.36 A ATOM 1301 CB ALA A 166 6.055 −1.944 56.520 1.00 10.05 A ATOM1302 C ALA A 166 7.832 −0.201 56.716 1.00 10.76 A ATOM 1303 O ALA A 1667.311 0.568 57.541 1.00 10.61 A ATOM 1304 N GLY A 167 9.142 −0.40456.660 1.00 10.33 A ATOM 1305 CA GLY A 167 10.025 0.363 57.525 1.0010.23 A ATOM 1306 C GLY A 167 9.945 1.808 57.056 1.00 10.55 A ATOM 1307O GLY A 167 10.031 2.757 57.844 1.00 9.84 A ATOM 1308 N GLY A 168 9.7791.982 55.749 1.00 9.79 A ATOM 1309 CA GLY A 168 9.650 3.319 55.205 1.0010.50 A ATOM 1310 C GLY A 168 8.246 3.849 55.466 1.00 9.99 A ATOM 1311 OGLY A 168 8.057 5.036 55.733 1.00 10.63 A ATOM 1312 N THR A 169 7.2602.957 55.392 1.00 9.91 A ATOM 1313 CA THR A 169 5.853 3.307 55.615 1.008.80 A ATOM 1314 CB THR A 169 4.939 2.060 55.439 1.00 9.40 A ATOM 1315OG1 THR A 169 5.186 1.457 54.163 1.00 10.04 A ATOM 1316 CG2 THR A 1693.468 2.454 55.521 1.00 9.30 A ATOM 1317 C THR A 169 5.590 3.898 57.0061.00 8.76 A ATOM 1318 O THR A 169 4.865 4.896 57.144 1.00 7.14 A ATOM1319 N VAL A 170 6.157 3.288 58.046 1.00 7.94 A ATOM 1320 CA VAL A 1705.925 3.804 59.391 1.00 7.96 A ATOM 1321 CB VAL A 170 6.391 2.818 60.4921.00 8.12 A ATOM 1322 CG1 VAL A 170 5.595 1.516 60.377 1.00 8.51 A ATOM1323 CG2 VAL A 170 7.894 2.571 60.387 1.00 8.83 A ATOM 1324 C VAL A 1706.599 5.153 59.615 1.00 8.27 A ATOM 1325 O VAL A 170 6.121 5.958 60.4111.00 8.24 A ATOM 1326 N LEU A 171 7.706 5.401 58.919 1.00 8.82 A ATOM1327 CA LEU A 171 8.398 6.680 59.059 1.00 9.31 A ATOM 1328 CB LEU A 1719.798 6.610 58.438 1.00 9.00 A ATOM 1329 CG LEU A 171 10.849 5.86359.275 1.00 9.38 A ATOM 1330 CD1 LEU A 171 12.115 5.666 58.461 1.0010.01 A ATOM 1331 CD2 LEU A 171 11.155 6.668 60.549 1.00 10.13 A ATOM1332 C LEU A 171 7.559 7.756 58.371 1.00 9.34 A ATOM 1333 O LEU A 1717.412 8.868 58.886 1.00 9.70 A ATOM 1334 N ARG A 172 7.006 7.411 57.2081.00 9.62 A ATOM 1335 CA ARG A 172 6.155 8.319 56.435 1.00 9.46 A ATOM1336 CB ARG A 172 5.757 7.647 55.106 1.00 10.16 A ATOM 1337 CG ARG A 1724.732 8.408 54.269 1.00 10.70 A ATOM 1338 CD ARG A 172 4.768 7.97152.792 1.00 10.81 A ATOM 1339 NE ARG A 172 4.534 6.538 52.581 1.00 10.35A ATOM 1340 CZ ARG A 172 3.341 5.948 52.574 1.00 10.72 A ATOM 1341 NH1ARG A 172 2.232 6.652 52.772 1.00 10.58 A ATOM 1342 NH2 ARG A 172 3.2514.641 52.336 1.00 10.24 A ATOM 1343 C ARG A 172 4.906 8.703 57.246 1.009.67 A ATOM 1344 O ARG A 172 4.491 9.864 57.251 1.00 8.96 A ATOM 1345 NLEU A 173 4.315 7.735 57.943 1.00 9.66 A ATOM 1346 CA LEU A 173 3.1358.015 58.759 1.00 9.61 A ATOM 1347 CB LEU A 173 2.469 6.714 59.221 1.0010.65 A ATOM 1348 CG LEU A 173 1.700 5.893 58.180 1.00 10.70 A ATOM 1349CD1 LEU A 173 1.374 4.522 58.764 1.00 10.48 A ATOM 1350 CD2 LEU A 1730.422 6.630 57.766 1.00 10.97 A ATOM 1351 C LEU A 173 3.514 8.846 59.9851.00 10.02 A ATOM 1352 O LEU A 173 2.838 9.819 60.314 1.00 8.14 A ATOM1353 N ALA A 174 4.589 8.452 60.667 1.00 9.18 A ATOM 1354 CA ALA A 1745.031 9.177 61.858 1.00 9.26 A ATOM 1355 CB ALA A 174 6.273 8.507 62.4531.00 8.76 A ATOM 1356 C ALA A 174 5.331 10.640 61.533 1.00 9.47 A ATOM1357 O ALA A 174 5.117 11.530 62.362 1.00 9.93 A ATOM 1358 N LYS A 1755.833 10.889 60.330 1.00 9.17 A ATOM 1359 CA LYS A 175 6.160 12.25259.925 1.00 9.55 A ATOM 1360 CB LYS A 175 6.749 12.262 58.509 1.00 9.91A ATOM 1361 CG LYS A 175 7.144 13.652 58.009 1.00 10.71 A ATOM 1362 CDLYS A 175 7.661 13.602 56.573 1.00 11.77 A ATOM 1363 CE LYS A 175 8.15214.967 56.104 1.00 11.36 A ATOM 1364 NZ LYS A 175 7.064 15.983 56.0221.00 12.68 A ATOM 1365 C LYS A 175 4.932 13.167 59.986 1.00 9.54 A ATOM1366 O LYS A 175 4.990 14.252 60.561 1.00 9.61 A ATOM 1367 N ASP A 1763.816 12.733 59.409 1.00 9.94 A ATOM 1368 CA ASP A 176 2.611 13.56359.437 1.00 10.35 A ATOM 1369 CB ASP A 176 1.577 13.062 58.422 1.0010.89 A ATOM 1370 CG ASP A 176 1.986 13.336 56.984 1.00 11.89 A ATOM1371 OD1 ASP A 176 2.750 14.301 56.755 1.00 12.55 A ATOM 1372 OD2 ASP A176 1.526 12.600 56.084 1.00 12.25 A ATOM 1373 C ASP A 176 1.953 13.65860.816 1.00 10.80 A ATOM 1374 O ASP A 176 1.484 14.729 61.206 1.00 11.51A ATOM 1375 N LEU A 177 1.913 12.558 61.563 1.00 10.38 A ATOM 1376 CALEU A 177 1.278 12.595 62.882 1.00 10.56 A ATOM 1377 CB LEU A 177 1.20611.190 63.502 1.00 11.79 A ATOM 1378 CG LEU A 177 0.639 9.991 62.7251.00 14.19 A ATOM 1379 CD1 LEU A 177 0.109 8.979 63.738 1.00 13.55 AATOM 1380 CD2 LEU A 177 −0.469 10.405 61.769 1.00 13.39 A ATOM 1381 CLEU A 177 2.012 13.535 63.845 1.00 10.13 A ATOM 1382 O LEU A 177 1.38114.256 64.613 1.00 10.07 A ATOM 1383 N ALA A 178 3.343 13.532 63.7981.00 9.17 A ATOM 1384 CA ALA A 178 4.132 14.387 64.684 1.00 9.84 A ATOM1385 CB ALA A 178 5.565 13.867 64.768 1.00 9.65 A ATOM 1386 C ALA A 1784.144 15.860 64.261 1.00 9.88 A ATOM 1387 O ALA A 178 4.064 16.75665.108 1.00 10.05 A ATOM 1388 N GLU A 179 4.243 16.111 62.958 1.00 9.81A ATOM 1389 CA GLU A 179 4.286 17.479 62.447 1.00 10.22 A ATOM 1390 CBGLU A 179 4.834 17.488 61.005 1.00 10.39 A ATOM 1391 CG GLU A 179 6.36317.310 60.920 1.00 12.08 A ATOM 1392 CD GLU A 179 6.887 17.099 59.4951.00 12.59 A ATOM 1393 OE1 GLU A 179 6.109 17.252 58.527 1.00 13.52 AATOM 1394 OE2 GLU A 179 8.090 16.781 59.344 1.00 11.85 A ATOM 1395 C GLUA 179 2.954 18.241 62.507 1.00 10.38 A ATOM 1396 O GLU A 179 2.95319.465 62.644 1.00 10.28 A ATOM 1397 N ASN A 180 1.828 17.534 62.4261.00 10.18 A ATOM 1398 CA ASN A 180 0.522 18.204 62.453 1.00 10.49 AATOM 1399 CB ASN A 180 −0.468 17.472 61.534 1.00 10.37 A ATOM 1400 CGASN A 180 −1.703 18.304 61.229 1.00 10.46 A ATOM 1401 OD1 ASN A 180−1.591 19.448 60.787 1.00 11.09 A ATOM 1402 ND2 ASN A 180 −2.888 17.73361.457 1.00 10.21 A ATOM 1403 C ASN A 180 −0.121 18.362 63.834 1.0010.50 A ATOM 1404 O ASN A 180 −1.202 18.945 63.944 1.00 10.62 A ATOM1405 N ASN A 181 0.535 17.860 64.880 1.00 10.99 A ATOM 1406 CA ASN A 181−0.016 17.927 66.238 1.00 11.61 A ATOM 1407 CB ASN A 181 −0.564 16.54966.625 1.00 10.99 A ATOM 1408 CG ASN A 181 −1.740 16.127 65.759 1.0011.32 A ATOM 1409 OD1 ASN A 181 −2.859 16.615 65.934 1.00 10.59 A ATOM1410 ND2 ASN A 181 −1.489 15.227 64.808 1.00 9.52 A ATOM 1411 C ASN A181 0.998 18.401 67.292 1.00 11.97 A ATOM 1412 O ASN A 181 1.937 17.67967.643 1.00 12.00 A ATOM 1413 N LYS A 182 0.795 19.614 67.798 1.00 12.75A ATOM 1414 CA LYS A 182 1.696 20.206 68.789 1.00 13.47 A ATOM 1415 CBLYS A 182 1.196 21.599 69.184 1.00 14.26 A ATOM 1416 CG LYS A 182 2.07922.332 70.192 1.00 15.00 A ATOM 1417 CD LYS A 182 1.552 23.747 70.4171.00 16.14 A ATOM 1418 CE LYS A 182 2.521 24.601 71.221 1.00 16.60 AATOM 1419 NZ LYS A 182 1.974 25.979 71.402 1.00 18.49 A ATOM 1420 C LYSA 182 1.856 19.357 70.044 1.00 13.44 A ATOM 1421 O LYS A 182 0.87218.987 70.684 1.00 13.52 A ATOM 1422 N GLY A 183 3.105 19.060 70.3911.00 13.68 A ATOM 1423 CA GLY A 183 3.383 18.262 71.574 1.00 13.42 AATOM 1424 C GLY A 183 3.351 16.758 71.360 1.00 12.95 A ATOM 1425 O GLY A183 3.689 15.993 72.259 1.00 13.54 A ATOM 1426 N ALA A 184 2.963 16.32070.169 1.00 13.05 A ATOM 1427 CA ALA A 184 2.875 14.891 69.893 1.0011.73 A ATOM 1428 CB ALA A 184 2.194 14.659 68.537 1.00 11.31 A ATOM1429 C ALA A 184 4.218 14.167 69.930 1.00 11.28 A ATOM 1430 O ALA A 1845.223 14.664 69.426 1.00 11.97 A ATOM 1431 N ARG A 185 4.216 12.99070.547 1.00 10.77 A ATOM 1432 CA ARG A 185 5.402 12.145 70.650 1.0010.15 A ATOM 1433 CB ARG A 185 5.943 12.158 72.085 1.00 10.47 A ATOM1434 CG ARG A 185 6.661 13.478 72.457 1.00 10.37 A ATOM 1435 CD ARG A185 7.966 13.635 71.667 1.00 11.21 A ATOM 1436 NE ARG A 185 8.724 14.85971.958 1.00 11.36 A ATOM 1437 CZ ARG A 185 8.514 16.039 71.375 1.0011.90 A ATOM 1438 NH1 ARG A 185 7.557 16.180 70.462 1.00 11.35 A ATOM1439 NH2 ARG A 185 9.287 17.078 71.676 1.00 12.08 A ATOM 1440 C ARG A185 4.937 10.754 70.219 1.00 9.96 A ATOM 1441 O ARG A 185 4.102 10.12170.878 1.00 8.97 A ATOM 1442 N VAL A 186 5.477 10.297 69.093 1.00 9.29 AATOM 1443 CA VAL A 186 5.083 9.024 68.499 1.00 9.31 A ATOM 1444 CB VAL A186 4.918 9.190 66.966 1.00 9.15 A ATOM 1445 CG1 VAL A 186 4.292 7.93366.360 1.00 9.74 A ATOM 1446 CG2 VAL A 186 4.063 10.423 66.659 1.00 9.08A ATOM 1447 C VAL A 186 6.026 7.852 68.742 1.00 9.11 A ATOM 1448 O VAL A186 7.213 7.930 68.423 1.00 8.24 A ATOM 1449 N LEU A 187 5.496 6.77469.325 1.00 9.01 A ATOM 1450 CA LEU A 187 6.293 5.570 69.547 1.00 8.10 AATOM 1451 CB LEU A 187 5.856 4.829 70.819 1.00 8.38 A ATOM 1452 CG LEU A187 6.458 3.432 71.043 1.00 7.36 A ATOM 1453 CD1 LEU A 187 7.982 3.52071.124 1.00 7.26 A ATOM 1454 CD2 LEU A 187 5.901 2.821 72.327 1.00 6.64A ATOM 1455 C LEU A 187 6.011 4.703 68.319 1.00 8.64 A ATOM 1456 O LEU A187 4.852 4.408 68.021 1.00 8.42 A ATOM 1457 N VAL A 188 7.069 4.32067.610 1.00 8.34 A ATOM 1458 CA VAL A 188 6.954 3.497 66.406 1.00 8.95 AATOM 1459 CB VAL A 188 7.675 4.163 65.208 1.00 8.81 A ATOM 1460 CG1 VALA 188 7.505 3.307 63.952 1.00 9.57 A ATOM 1461 CG2 VAL A 188 7.127 5.56364.983 1.00 8.73 A ATOM 1462 C VAL A 188 7.603 2.144 66.665 1.00 9.22 AATOM 1463 O VAL A 188 8.750 2.089 67.109 1.00 9.45 A ATOM 1464 N VAL A189 6.876 1.059 66.389 1.00 9.29 A ATOM 1465 CA VAL A 189 7.403 −0.28666.609 1.00 9.54 A ATOM 1466 CB VAL A 189 6.771 −0.938 67.876 1.00 9.93A ATOM 1467 CG1 VAL A 189 7.359 −2.339 68.101 1.00 10.83 A ATOM 1468 CG2VAL A 189 7.006 −0.060 69.103 1.00 10.08 A ATOM 1469 C VAL A 189 7.180−1.250 65.437 1.00 9.89 A ATOM 1470 O VAL A 189 6.044 −1.446 64.985 1.009.62 A ATOM 1471 N CYS A 190 8.267 −1.838 64.944 1.00 10.01 A ATOM 1472CA CYS A 190 8.194 −2.838 63.875 1.00 10.09 A ATOM 1473 CB CYS A 1909.120 −2.495 62.703 1.00 11.33 A ATOM 1474 SG CYS A 190 8.653 −1.05961.716 1.00 12.55 A ATOM 1475 C CYS A 190 8.680 −4.130 64.530 1.00 10.56A ATOM 1476 O CYS A 190 9.794 −4.182 65.062 1.00 9.40 A ATOM 1477 N SERA 191 7.847 −5.165 64.498 1.00 10.19 A ATOM 1478 CA SER A 191 8.193−6.448 65.106 1.00 10.68 A ATOM 1479 CB SER A 191 7.402 −6.629 66.4051.00 10.50 A ATOM 1480 OG SER A 191 7.696 −7.867 67.016 1.00 10.11 AATOM 1481 C SER A 191 7.863 −7.573 64.137 1.00 10.91 A ATOM 1482 O SER A191 6.706 −7.740 63.750 1.00 10.99 A ATOM 1483 N GLU A 192 8.876 −8.35163.760 1.00 11.05 A ATOM 1484 CA GLU A 192 8.699 −9.442 62.800 1.0010.62 A ATOM 1485 CB GLU A 192 9.462 −9.107 61.512 1.00 10.66 A ATOM1486 CG GLU A 192 9.135 −7.721 60.914 1.00 10.64 A ATOM 1487 CD GLU A192 7.802 −7.684 60.166 1.00 10.87 A ATOM 1488 OE1 GLU A 192 7.109−8.719 60.125 1.00 11.53 A ATOM 1489 OE2 GLU A 192 7.446 −6.618 59.6181.00 10.92 A ATOM 1490 C GLU A 192 9.170 −10.796 63.347 1.00 10.89 AATOM 1491 O GLU A 192 10.285 −10.917 63.847 1.00 9.91 A ATOM 1492 N VALA 193 8.316 −11.811 63.221 1.00 11.07 A ATOM 1493 CA VAL A 193 8.602−13.162 63.711 1.00 11.62 A ATOM 1494 CB VAL A 193 7.725 −13.468 64.9531.00 11.44 A ATOM 1495 CG1 VAL A 193 7.933 −14.908 65.420 1.00 11.03 AATOM 1496 CG2 VAL A 193 8.074 −12.489 66.077 1.00 11.56 A ATOM 1497 CVAL A 193 8.328 −14.197 62.614 1.00 12.46 A ATOM 1498 O VAL A 193 7.192−14.331 62.151 1.00 12.86 A ATOM 1499 N THR A 194 9.366 −14.933 62.2161.00 12.81 A ATOM 1500 CA THR A 194 9.260 −15.931 61.148 1.00 12.86 AATOM 1501 CB THR A 194 10.664 −16.424 60.702 1.00 13.15 A ATOM 1502 OG1THR A 194 11.370 −16.975 61.822 1.00 12.89 A ATOM 1503 CG2 THR A 19411.472 −15.264 60.112 1.00 13.13 A ATOM 1504 C THR A 194 8.381 −17.16061.395 1.00 13.30 A ATOM 1505 O THR A 194 8.258 −18.017 60.519 1.0012.89 A ATOM 1506 N ALA A 195 7.775 −17.256 62.571 1.00 13.76 A ATOM1507 CA ALA A 195 6.897 −18.384 62.872 1.00 14.53 A ATOM 1508 CB ALA A195 6.322 −18.242 64.278 1.00 15.45 A ATOM 1509 C ALA A 195 5.758−18.440 61.855 1.00 14.54 A ATOM 1510 O ALA A 195 5.173 −19.498 61.6121.00 14.97 A ATOM 1511 N VAL A 196 5.445 −17.296 61.260 1.00 14.30 AATOM 1512 CA VAL A 196 4.363 −17.231 60.289 1.00 14.81 A ATOM 1513 CBVAL A 196 3.774 −15.792 60.215 1.00 14.74 A ATOM 1514 CG1 VAL A 1964.742 −14.859 59.494 1.00 15.82 A ATOM 1515 CG2 VAL A 196 2.412 −15.81659.525 1.00 15.91 A ATOM 1516 C VAL A 196 4.770 −17.696 58.884 1.0014.53 A ATOM 1517 O VAL A 196 3.914 −18.082 58.088 1.00 14.83 A ATOM1518 N THR A 197 6.069 −17.694 58.589 1.00 14.33 A ATOM 1519 CA THR A197 6.542 −18.097 57.263 1.00 14.12 A ATOM 1520 CB THR A 197 7.393−16.975 56.603 1.00 14.84 A ATOM 1521 OG1 THR A 197 8.492 −16.640 57.4601.00 14.20 A ATOM 1522 CG2 THR A 197 6.548 −15.736 56.346 1.00 14.92 AATOM 1523 C THR A 197 7.361 −19.392 57.184 1.00 13.95 A ATOM 1524 O THRA 197 7.515 −19.951 56.099 1.00 14.12 A ATOM 1525 N PHE A 198 7.891−19.868 58.309 1.00 13.34 A ATOM 1526 CA PHE A 198 8.705 −21.089 58.2951.00 13.23 A ATOM 1527 CB PHE A 198 9.239 −21.393 59.706 1.00 12.64 AATOM 1528 CG PHE A 198 10.107 −22.633 59.782 1.00 12.39 A ATOM 1529 CD1PHE A 198 9.538 −23.904 59.752 1.00 12.24 A ATOM 1530 CD2 PHE A 19811.495 −22.524 59.849 1.00 12.72 A ATOM 1531 CE1 PHE A 198 10.336−25.054 59.783 1.00 12.32 A ATOM 1532 CE2 PHE A 198 12.306 −23.66859.880 1.00 12.12 A ATOM 1533 CZ PHE A 198 11.720 −24.936 59.846 1.0012.30 A ATOM 1534 C PHE A 198 7.958 −22.310 57.764 1.00 13.09 A ATOM1535 O PHE A 198 6.816 −22.572 58.152 1.00 12.80 A ATOM 1536 N ARG A 1998.609 −23.060 56.877 1.00 13.29 A ATOM 1537 CA ARG A 199 8.012 −24.27556.323 1.00 13.07 A ATOM 1538 CB ARG A 199 6.925 −23.922 55.293 1.0013.33 A ATOM 1539 CG ARG A 199 7.405 −23.140 54.078 1.00 12.99 A ATOM1540 CD ARG A 199 6.224 −22.551 53.305 1.00 13.81 A ATOM 1541 NE ARG A199 5.473 −21.575 54.101 1.00 13.90 A ATOM 1542 CZ ARG A 199 4.324−21.820 54.734 1.00 13.37 A ATOM 1543 NH1 ARG A 199 3.757 −23.020 54.6821.00 12.59 A ATOM 1544 NH2 ARG A 199 3.735 −20.854 55.424 1.00 12.86 AATOM 1545 C ARG A 199 9.076 −25.183 55.702 1.00 13.44 A ATOM 1546 O ARGA 199 10.198 −24.749 55.446 1.00 12.86 A ATOM 1547 N GLY A 200 8.717−26.447 55.479 1.00 14.16 A ATOM 1548 CA GLY A 200 9.647 −27.412 54.9081.00 14.89 A ATOM 1549 C GLY A 200 10.055 −27.114 53.476 1.00 15.67 AATOM 1550 O GLY A 200 9.433 −26.282 52.820 1.00 15.33 A ATOM 1551 N PROA 201 11.101 −27.789 52.962 1.00 16.65 A ATOM 1552 CD PRO A 201 11.997−28.662 53.747 1.00 16.48 A ATOM 1553 CA PRO A 201 11.616 −27.610 51.6001.00 17.08 A ATOM 1554 CB PRO A 201 13.059 −28.084 51.724 1.00 16.70 AATOM 1555 CG PRO A 201 12.923 −29.231 52.681 1.00 17.23 A ATOM 1556 CPRO A 201 10.861 −28.372 50.514 1.00 18.19 A ATOM 1557 O PRO A 20110.369 −29.475 50.748 1.00 18.52 A ATOM 1558 N SER A 202 10.788 −27.77749.325 1.00 19.20 A ATOM 1559 CA SER A 202 10.112 −28.381 48.171 1.0020.83 A ATOM 1560 CB SER A 202 8.714 −27.777 48.003 1.00 20.75 A ATOM1561 OG SER A 202 8.080 −28.273 46.833 1.00 22.13 A ATOM 1562 C SER A202 10.939 −28.131 46.906 1.00 21.36 A ATOM 1563 O SER A 202 11.276−26.988 46.601 1.00 21.26 A ATOM 1564 N ASP A 203 11.259 −29.188 46.1621.00 22.79 A ATOM 1565 CA ASP A 203 12.071 −29.018 44.958 1.00 24.44 AATOM 1566 CB ASP A 203 12.717 −30.349 44.543 1.00 25.63 A ATOM 1567 CGASP A 203 11.705 −31.429 44.235 1.00 27.41 A ATOM 1568 OD1 ASP A 20312.134 −32.575 43.975 1.00 29.04 A ATOM 1569 OD2 ASP A 203 10.490−31.143 44.249 1.00 28.72 A ATOM 1570 C ASP A 203 11.345 −28.383 43.7741.00 24.57 A ATOM 1571 O ASP A 203 11.938 −28.183 42.714 1.00 25.13 AATOM 1572 N THR A 204 10.070 −28.055 43.952 1.00 24.84 A ATOM 1573 CATHR A 204 9.307 −27.406 42.892 1.00 25.35 A ATOM 1574 CB THR A 204 7.995−28.171 42.574 1.00 25.57 A ATOM 1575 OG1 THR A 204 7.270 −28.430 43.7841.00 26.36 A ATOM 1576 CG2 THR A 204 8.309 −29.491 41.878 1.00 25.89 AATOM 1577 C THR A 204 8.980 −25.962 43.290 1.00 25.30 A ATOM 1578 O THRA 204 8.263 −25.253 42.579 1.00 24.92 A ATOM 1579 N HIS A 205 9.520−25.533 44.429 1.00 25.03 A ATOM 1580 CA HIS A 205 9.308 −24.175 44.9241.00 25.38 A ATOM 1581 CB HIS A 205 8.244 −24.166 46.026 1.00 26.03 AATOM 1582 CG HIS A 205 6.916 −24.699 45.585 1.00 26.52 A ATOM 1583 CD2HIS A 205 5.865 −24.087 44.989 1.00 27.09 A ATOM 1584 ND1 HIS A 2056.571 −26.029 45.698 1.00 26.88 A ATOM 1585 CE1 HIS A 205 5.366 −26.21445.189 1.00 26.94 A ATOM 1586 NE2 HIS A 205 4.915 −25.051 44.751 1.0027.31 A ATOM 1587 C HIS A 205 10.609 −23.584 45.461 1.00 25.22 A ATOM1588 O HIS A 205 10.719 −23.267 46.643 1.00 25.50 A ATOM 1589 N LEU A206 11.591 −23.425 44.579 1.00 24.95 A ATOM 1590 CA LEU A 206 12.892−22.890 44.963 1.00 24.94 A ATOM 1591 CB LEU A 206 13.863 −22.992 43.7811.00 24.92 A ATOM 1592 CG LEU A 206 14.102 −24.420 43.264 1.00 25.37 AATOM 1593 CD1 LEU A 206 15.120 −24.397 42.129 1.00 25.23 A ATOM 1594 CD2LEU A 206 14.591 −25.313 44.404 1.00 24.70 A ATOM 1595 C LEU A 20612.850 −21.455 45.495 1.00 25.23 A ATOM 1596 O LEU A 206 13.729 −21.04746.257 1.00 24.95 A ATOM 1597 N ASP A 207 11.832 −20.690 45.104 1.0025.29 A ATOM 1598 CA ASP A 207 11.709 −19.317 45.583 1.00 25.66 A ATOM1599 CB ASP A 207 10.656 −18.548 44.775 1.00 27.12 A ATOM 1600 CG ASP A207 9.299 −19.231 44.768 1.00 28.64 A ATOM 1601 OD1 ASP A 207 8.347−18.634 44.222 1.00 29.73 A ATOM 1602 OD2 ASP A 207 9.178 −20.360 45.2941.00 29.96 A ATOM 1603 C ASP A 207 11.341 −19.309 47.065 1.00 25.27 AATOM 1604 O ASP A 207 11.753 −18.426 47.817 1.00 25.41 A ATOM 1605 N SERA 208 10.567 −20.301 47.486 1.00 24.29 A ATOM 1606 CA SER A 208 10.173−20.399 48.881 1.00 23.76 A ATOM 1607 CB SER A 208 9.090 −21.473 49.0481.00 24.07 A ATOM 1608 OG SER A 208 8.686 −21.592 50.400 1.00 25.22 AATOM 1609 C SER A 208 11.409 −20.761 49.704 1.00 22.63 A ATOM 1610 O SERA 208 11.607 −20.258 50.809 1.00 22.30 A ATOM 1611 N LEU A 209 12.251−21.620 49.138 1.00 21.70 A ATOM 1612 CA LEU A 209 13.464 −22.075 49.8021.00 20.71 A ATOM 1613 CB LEU A 209 14.136 −23.165 48.957 1.00 20.77 AATOM 1614 CG LEU A 209 15.193 −24.039 49.629 1.00 20.98 A ATOM 1615 CD1LEU A 209 14.554 −24.802 50.786 1.00 20.75 A ATOM 1616 CD2 LEU A 20915.786 −25.009 48.608 1.00 20.81 A ATOM 1617 C LEU A 209 14.461 −20.95050.078 1.00 20.48 A ATOM 1618 O LEU A 209 15.090 −20.924 51.139 1.0020.50 A ATOM 1619 N VAL A 210 14.621 −20.029 49.131 1.00 19.42 A ATOM1620 CA VAL A 210 15.560 −18.929 49.329 1.00 19.15 A ATOM 1621 CB VAL A210 15.658 −18.009 48.080 1.00 19.36 A ATOM 1622 CG1 VAL A 210 14.353−17.264 47.857 1.00 20.36 A ATOM 1623 CG2 VAL A 210 16.806 −17.02548.251 1.00 20.35 A ATOM 1624 C VAL A 210 15.123 −18.119 50.545 1.0018.35 A ATOM 1625 O VAL A 210 15.954 −17.608 51.289 1.00 18.00 A ATOM1626 N GLY A 211 13.812 −18.016 50.742 1.00 17.76 A ATOM 1627 CA GLY A211 13.288 −17.295 51.888 1.00 17.42 A ATOM 1628 C GLY A 211 13.710−17.941 53.202 1.00 16.84 A ATOM 1629 O GLY A 211 13.903 −17.249 54.2011.00 17.07 A ATOM 1630 N GLN A 212 13.855 −19.265 53.207 1.00 16.19 AATOM 1631 CA GLN A 212 14.267 −19.979 54.415 1.00 16.19 A ATOM 1632 CBGLN A 212 14.053 −21.491 54.250 1.00 16.68 A ATOM 1633 CG GLN A 21212.614 −21.917 53.927 1.00 18.07 A ATOM 1634 CD GLN A 212 11.600 −21.43654.954 1.00 18.95 A ATOM 1635 OE1 GLN A 212 11.761 −21.657 56.152 1.0019.82 A ATOM 1636 NE2 GLN A 212 10.547 −20.779 54.485 1.00 19.27 A ATOM1637 C GLN A 212 15.741 −19.702 54.741 1.00 15.86 A ATOM 1638 O GLN A212 16.191 −19.908 55.869 1.00 15.74 A ATOM 1639 N ALA A 213 16.492−19.231 53.751 1.00 15.43 A ATOM 1640 CA ALA A 213 17.904 −18.922 53.9531.00 15.06 A ATOM 1641 CB ALA A 213 18.686 −19.225 52.674 1.00 15.32 AATOM 1642 C ALA A 213 18.137 −17.463 54.365 1.00 14.68 A ATOM 1643 O ALAA 213 19.204 −17.117 54.886 1.00 14.33 A ATOM 1644 N LEU A 214 17.135−16.616 54.154 1.00 14.29 A ATOM 1645 CA LEU A 214 17.275 −15.192 54.4551.00 14.48 A ATOM 1646 CB LEU A 214 16.924 −14.378 53.205 1.00 14.91 AATOM 1647 CG LEU A 214 17.668 −14.670 51.901 1.00 15.41 A ATOM 1648 CD1LEU A 214 17.042 −13.844 50.774 1.00 16.41 A ATOM 1649 CD2 LEU A 21419.146 −14.341 52.058 1.00 16.05 A ATOM 1650 C LEU A 214 16.520 −14.57655.640 1.00 14.29 A ATOM 1651 O LEU A 214 17.082 −13.739 56.351 1.0014.63 A ATOM 1652 N PHE A 215 15.264 −14.965 55.844 1.00 13.93 A ATOM1653 CA PHE A 215 14.440 −14.377 56.907 1.00 13.96 A ATOM 1654 CB PHE A215 12.961 −14.752 56.718 1.00 15.54 A ATOM 1655 CG PHE A 215 12.433−14.517 55.324 1.00 17.87 A ATOM 1656 CD1 PHE A 215 12.952 −13.50754.519 1.00 18.86 A ATOM 1657 CD2 PHE A 215 11.395 −15.302 54.826 1.0018.79 A ATOM 1658 CE1 PHE A 215 12.445 −13.283 53.234 1.00 19.31 A ATOM1659 CE2 PHE A 215 10.882 −15.086 53.547 1.00 19.39 A ATOM 1660 CZ PHE A215 11.409 −14.074 52.750 1.00 19.43 A ATOM 1661 C PHE A 215 14.826−14.689 58.349 1.00 13.33 A ATOM 1662 O PHE A 215 15.054 −15.847 58.7041.00 12.97 A ATOM 1663 N GLY A 216 14.859 −13.637 59.170 1.00 12.63 AATOM 1664 CA GLY A 216 15.195 −13.751 60.585 1.00 12.55 A ATOM 1665 CGLY A 216 14.239 −12.912 61.429 1.00 12.18 A ATOM 1666 O GLY A 21613.452 −12.136 60.873 1.00 11.45 A ATOM 1667 N ASP A 217 14.313 −13.05062.757 1.00 11.54 A ATOM 1668 CA ASP A 217 13.430 −12.325 63.687 1.0011.59 A ATOM 1669 CB ASP A 217 12.952 −13.267 64.798 1.00 11.47 A ATOM1670 CG ASP A 217 12.188 −14.469 64.275 1.00 12.37 A ATOM 1671 OD1 ASP A217 12.114 −14.667 63.043 1.00 12.95 A ATOM 1672 OD2 ASP A 217 11.665−15.227 65.112 1.00 13.04 A ATOM 1673 C ASP A 217 14.046 −11.089 64.3621.00 11.79 A ATOM 1674 O ASP A 217 15.253 −11.040 64.619 1.00 11.06 AATOM 1675 N GLY A 218 13.196 −10.109 64.681 1.00 11.39 A ATOM 1676 CAGLY A 218 13.666 −8.899 65.338 1.00 10.97 A ATOM 1677 C GLY A 218 12.637−7.786 65.469 1.00 11.12 A ATOM 1678 O GLY A 218 11.619 −7.780 64.7741.00 11.86 A ATOM 1679 N ALA A 219 12.894 −6.850 66.379 1.00 10.90 AATOM 1680 CA ALA A 219 12.010 −5.702 66.587 1.00 10.79 A ATOM 1681 CBALA A 219 11.083 −5.943 67.792 1.00 10.28 A ATOM 1682 C ALA A 219 12.848−4.439 66.811 1.00 10.65 A ATOM 1683 O ALA A 219 13.940 −4.496 67.3881.00 10.66 A ATOM 1684 N ALA A 220 12.333 −3.309 66.337 1.00 9.85 A ATOM1685 CA ALA A 220 13.002 −2.019 66.486 1.00 10.37 A ATOM 1686 CB ALA A220 13.677 −1.616 65.172 1.00 9.86 A ATOM 1687 C ALA A 220 11.959 −0.97966.887 1.00 10.57 A ATOM 1688 O ALA A 220 10.824 −1.007 66.399 1.0010.66 A ATOM 1689 N ALA A 221 12.339 −0.068 67.781 1.00 9.94 A ATOM 1690CA ALA A 221 11.419 0.963 68.246 1.00 10.32 A ATOM 1691 CB ALA A 22110.959 0.653 69.680 1.00 10.35 A ATOM 1692 C ALA A 221 12.045 2.35268.192 1.00 10.54 A ATOM 1693 O ALA A 221 13.237 2.518 68.475 1.00 9.74A ATOM 1694 N LEU A 222 11.223 3.341 67.840 1.00 10.56 A ATOM 1695 CALEU A 222 11.664 4.731 67.735 1.00 11.43 A ATOM 1696 CB LEU A 222 11.6765.180 66.269 1.00 12.57 A ATOM 1697 CG LEU A 222 12.161 4.265 65.1511.00 13.60 A ATOM 1698 CD1 LEU A 222 11.614 4.787 63.819 1.00 13.87 AATOM 1699 CD2 LEU A 222 13.681 4.204 65.138 1.00 12.89 A ATOM 1700 C LEUA 222 10.704 5.672 68.459 1.00 11.56 A ATOM 1701 O LEU A 222 9.532 5.34168.669 1.00 12.07 A ATOM 1702 N ILE A 223 11.216 6.838 68.848 1.00 11.46A ATOM 1703 CA ILE A 223 10.393 7.887 69.447 1.00 11.36 A ATOM 1704 CBILE A 223 10.904 8.370 70.829 1.00 11.65 A ATOM 1705 CG2 ILE A 22310.178 9.655 71.223 1.00 10.99 A ATOM 1706 CG1 ILE A 223 10.687 7.28971.893 1.00 11.08 A ATOM 1707 CD1 ILE A 223 9.227 6.989 72.214 1.0012.35 A ATOM 1708 C ILE A 223 10.588 9.011 68.435 1.00 11.23 A ATOM 1709O ILE A 223 11.726 9.402 68.149 1.00 11.56 A ATOM 1710 N VAL A 224 9.4869.509 67.879 1.00 10.50 A ATOM 1711 CA VAL A 224 9.522 10.570 66.8761.00 10.56 A ATOM 1712 CB VAL A 224 8.947 10.078 65.519 1.00 9.92 A ATOM1713 CG1 VAL A 224 8.933 11.223 64.499 1.00 9.91 A ATOM 1714 CG2 VAL A224 9.770 8.915 64.999 1.00 9.84 A ATOM 1715 C VAL A 224 8.705 11.78267.310 1.00 10.99 A ATOM 1716 O VAL A 224 7.578 11.644 67.789 1.00 10.91A ATOM 1717 N GLY A 225 9.276 12.970 67.135 1.00 11.59 A ATOM 1718 CAGLY A 225 8.567 14.181 67.499 1.00 11.11 A ATOM 1719 C GLY A 225 9.12615.444 66.874 1.00 11.82 A ATOM 1720 O GLY A 225 10.297 15.500 66.4881.00 10.35 A ATOM 1721 N SER A 226 8.273 16.457 66.761 1.00 12.29 A ATOM1722 CA SER A 226 8.676 17.755 66.230 1.00 13.04 A ATOM 1723 CB SER A226 7.557 18.364 65.376 1.00 13.32 A ATOM 1724 OG SER A 226 7.422 17.69764.133 1.00 14.87 A ATOM 1725 C SER A 226 8.940 18.661 67.437 1.00 13.71A ATOM 1726 O SER A 226 8.429 18.406 68.533 1.00 13.89 A ATOM 1727 N ASPA 227 9.746 19.701 67.240 1.00 13.96 A ATOM 1728 CA ASP A 227 10.05620.659 68.304 1.00 14.97 A ATOM 1729 CB ASP A 227 8.775 21.400 68.7111.00 15.35 A ATOM 1730 CG ASP A 227 7.974 21.886 67.512 1.00 15.96 AATOM 1731 OD1 ASP A 227 8.588 22.393 66.551 1.00 16.70 A ATOM 1732 OD2ASP A 227 6.729 21.766 67.536 1.00 17.02 A ATOM 1733 C ASP A 227 10.70520.040 69.549 1.00 15.00 A ATOM 1734 O ASP A 227 10.144 20.093 70.6461.00 14.00 A ATOM 1735 N PRO A 228 11.906 19.458 69.398 1.00 15.76 AATOM 1736 CD PRO A 228 12.704 19.370 68.165 1.00 16.05 A ATOM 1737 CAPRO A 228 12.614 18.832 70.524 1.00 16.49 A ATOM 1738 CB PRO A 22813.862 18.230 69.868 1.00 16.50 A ATOM 1739 CG PRO A 228 13.500 18.12468.405 1.00 17.67 A ATOM 1740 C PRO A 228 12.996 19.845 71.605 1.0016.81 A ATOM 1741 O PRO A 228 13.345 20.982 71.296 1.00 16.80 A ATOM1742 N VAL A 229 12.936 19.432 72.868 1.00 17.75 A ATOM 1743 CA VAL A229 13.307 20.311 73.972 1.00 18.66 A ATOM 1744 CB VAL A 229 12.75919.777 75.319 1.00 18.87 A ATOM 1745 CG1 VAL A 229 13.106 20.735 76.4421.00 18.50 A ATOM 1746 CG2 VAL A 229 11.252 19.587 75.231 1.00 19.24 AATOM 1747 C VAL A 229 14.842 20.357 74.024 1.00 19.25 A ATOM 1748 O VALA 229 15.490 19.361 74.338 1.00 19.01 A ATOM 1749 N PRO A 230 15.44021.516 73.703 1.00 19.93 A ATOM 1750 CD PRO A 230 14.785 22.779 73.3221.00 20.33 A ATOM 1751 CA PRO A 230 16.898 21.673 73.713 1.00 20.52 AATOM 1752 CB PRO A 230 17.082 23.173 73.500 1.00 20.70 A ATOM 1753 CGPRO A 230 15.912 23.527 72.641 1.00 20.85 A ATOM 1754 C PRO A 230 17.58521.188 74.986 1.00 21.15 A ATOM 1755 O PRO A 230 17.133 21.471 76.0921.00 20.91 A ATOM 1756 N GLU A 231 18.677 20.450 74.807 1.00 21.72 AATOM 1757 CA GLU A 231 19.474 19.921 75.914 1.00 22.87 A ATOM 1758 CBGLU A 231 19.977 21.072 76.790 1.00 24.06 A ATOM 1759 CG GLU A 23120.632 22.204 76.014 1.00 26.41 A ATOM 1760 CD GLU A 231 21.929 21.79575.342 1.00 28.22 A ATOM 1761 OE1 GLU A 231 22.428 22.575 74.502 1.0029.91 A ATOM 1762 OE2 GLU A 231 22.458 20.705 75.654 1.00 29.36 A ATOM1763 C GLU A 231 18.778 18.879 76.792 1.00 22.51 A ATOM 1764 O GLU A 23119.405 18.321 77.693 1.00 23.39 A ATOM 1765 N ILE A 232 17.492 18.62676.548 1.00 21.33 A ATOM 1766 CA ILE A 232 16.744 17.622 77.314 1.0020.10 A ATOM 1767 CB ILE A 232 15.372 18.165 77.808 1.00 20.35 A ATOM1768 CG2 ILE A 232 14.505 17.021 78.323 1.00 20.81 A ATOM 1769 CG1 ILE A232 15.588 19.189 78.927 1.00 20.76 A ATOM 1770 CD1 ILE A 232 16.38118.652 80.107 1.00 20.81 A ATOM 1771 C ILE A 232 16.511 16.406 76.4181.00 19.24 A ATOM 1772 O ILE A 232 16.779 15.270 76.808 1.00 18.76 AATOM 1773 N GLU A 233 15.998 16.654 75.218 1.00 18.19 A ATOM 1774 CA GLUA 233 15.773 15.588 74.248 1.00 17.68 A ATOM 1775 CB GLU A 233 14.43515.796 73.516 1.00 16.61 A ATOM 1776 CG GLU A 233 13.225 15.614 74.4421.00 15.77 A ATOM 1777 CD GLU A 233 11.878 15.811 73.763 1.00 15.66 AATOM 1778 OE1 GLU A 233 11.663 16.888 73.164 1.00 14.98 A ATOM 1779 OE2GLU A 233 11.024 14.894 73.846 1.00 13.88 A ATOM 1780 C GLU A 233 16.96915.696 73.304 1.00 18.08 A ATOM 1781 O GLU A 233 17.581 16.763 73.2021.00 18.12 A ATOM 1782 N LYS A 234 17.316 14.606 72.626 1.00 18.13 AATOM 1783 CA LYS A 234 18.479 14.620 71.743 1.00 18.28 A ATOM 1784 CBLYS A 234 19.609 13.818 72.391 1.00 19.97 A ATOM 1785 CG LYS A 23420.833 13.658 71.517 1.00 22.36 A ATOM 1786 CD LYS A 234 21.912 12.86472.228 1.00 24.07 A ATOM 1787 CE LYS A 234 23.161 12.748 71.377 1.0024.43 A ATOM 1788 NZ LYS A 234 24.241 12.063 72.132 1.00 26.13 A ATOM1789 C LYS A 234 18.226 14.088 70.332 1.00 17.50 A ATOM 1790 O LYS A 23418.151 12.879 70.117 1.00 17.33 A ATOM 1791 N PRO A 235 18.103 14.99569.349 1.00 16.44 A ATOM 1792 CD PRO A 235 18.018 16.454 69.532 1.0016.79 A ATOM 1793 CA PRO A 235 17.861 14.628 67.948 1.00 15.90 A ATOM1794 CB PRO A 235 17.822 15.983 67.244 1.00 16.17 A ATOM 1795 CG PRO A235 17.250 16.890 68.297 1.00 17.19 A ATOM 1796 C PRO A 235 18.94813.719 67.365 1.00 15.14 A ATOM 1797 O PRO A 235 20.133 13.916 67.6421.00 15.33 A ATOM 1798 N ILE A 236 18.540 12.739 66.559 1.00 13.84 AATOM 1799 CA ILE A 236 19.475 11.815 65.914 1.00 13.10 A ATOM 1800 CBILE A 236 19.117 10.335 66.217 1.00 12.82 A ATOM 1801 CG2 ILE A 23620.170 9.416 65.618 1.00 13.36 A ATOM 1802 CG1 ILE A 236 19.028 10.10467.727 1.00 12.98 A ATOM 1803 CD1 ILE A 236 18.623 8.689 68.107 1.0013.32 A ATOM 1804 C ILE A 236 19.454 12.029 64.389 1.00 12.89 A ATOM1805 O ILE A 236 20.503 12.188 63.760 1.00 12.73 A ATOM 1806 N PHE A 23718.254 12.019 63.808 1.00 12.93 A ATOM 1807 CA PHE A 237 18.052 12.23362.372 1.00 13.23 A ATOM 1808 CB PHE A 237 17.878 10.894 61.631 1.0013.29 A ATOM 1809 CG PHE A 237 19.118 10.037 61.594 1.00 13.07 A ATOM1810 CD1 PHE A 237 20.214 10.398 60.812 1.00 13.37 A ATOM 1811 CD2 PHE A237 19.183 8.860 62.334 1.00 13.32 A ATOM 1812 CE1 PHE A 237 21.3599.594 60.769 1.00 13.12 A ATOM 1813 CE2 PHE A 237 20.321 8.050 62.3001.00 13.01 A ATOM 1814 CZ PHE A 237 21.411 8.418 61.515 1.00 13.20 AATOM 1815 C PHE A 237 16.769 13.057 62.185 1.00 13.74 A ATOM 1816 O PHEA 237 15.818 12.909 62.953 1.00 14.05 A ATOM 1817 N GLU A 238 16.74413.917 61.170 1.00 14.11 A ATOM 1818 CA GLU A 238 15.558 14.728 60.8731.00 14.73 A ATOM 1819 CB GLU A 238 15.917 16.213 60.718 1.00 15.82 AATOM 1820 CG GLU A 238 16.429 16.918 61.958 1.00 18.71 A ATOM 1821 CDGLU A 238 16.434 18.438 61.794 1.00 21.33 A ATOM 1822 OE1 GLU A 23817.008 18.939 60.803 1.00 22.01 A ATOM 1823 OE2 GLU A 238 15.856 19.13562.657 1.00 22.77 A ATOM 1824 C GLU A 238 14.963 14.251 59.548 1.0014.20 A ATOM 1825 O GLU A 238 15.707 13.948 58.614 1.00 13.90 A ATOM1826 N MET A 239 13.638 14.180 59.456 1.00 13.86 A ATOM 1827 CA MET A239 13.008 13.766 58.205 1.00 14.51 A ATOM 1828 CB MET A 239 11.70213.006 58.468 1.00 15.35 A ATOM 1829 CG MET A 239 11.940 11.583 58.9701.00 17.08 A ATOM 1830 SD MET A 239 10.448 10.564 59.044 1.00 19.48 AATOM 1831 CE MET A 239 9.981 10.786 60.745 1.00 18.17 A ATOM 1832 C META 239 12.757 15.011 57.363 1.00 14.60 A ATOM 1833 O MET A 239 12.32916.047 57.884 1.00 13.98 A ATOM 1834 N VAL A 240 13.041 14.905 56.0671.00 14.28 A ATOM 1835 CA VAL A 240 12.893 16.025 55.141 1.00 15.20 AATOM 1836 CB VAL A 240 14.224 16.271 54.375 1.00 15.56 A ATOM 1837 CG1VAL A 240 14.091 17.470 53.452 1.00 15.90 A ATOM 1838 CG2 VAL A 24015.366 16.479 55.363 1.00 16.93 A ATOM 1839 C VAL A 240 11.784 15.87554.096 1.00 15.14 A ATOM 1840 O VAL A 240 11.009 16.803 53.865 1.0014.78 A ATOM 1841 N TRP A 241 11.715 14.706 53.466 1.00 15.48 A ATOM1842 CA TRP A 241 10.740 14.462 52.405 1.00 15.48 A ATOM 1843 CB TRP A241 11.309 15.035 51.104 1.00 17.25 A ATOM 1844 CG TRP A 241 10.44614.908 49.891 1.00 18.55 A ATOM 1845 CD2 TRP A 241 10.627 13.993 48.8021.00 19.60 A ATOM 1846 CE2 TRP A 241 9.618 14.267 47.851 1.00 20.24 AATOM 1847 CE3 TRP A 241 11.544 12.968 48.536 1.00 19.96 A ATOM 1848 CD1TRP A 241 9.363 15.674 49.571 1.00 19.19 A ATOM 1849 NE1 TRP A 241 8.86015.296 48.345 1.00 20.36 A ATOM 1850 CZ2 TRP A 241 9.503 13.554 46.6521.00 20.07 A ATOM 1851 CZ3 TRP A 241 11.428 12.259 47.344 1.00 20.26 AATOM 1852 CH2 TRP A 241 10.414 12.559 46.417 1.00 20.45 A ATOM 1853 CTRP A 241 10.500 12.958 52.252 1.00 15.29 A ATOM 1854 O TRP A 241 11.39912.162 52.516 1.00 15.20 A ATOM 1855 N THR A 242 9.297 12.570 51.8271.00 14.37 A ATOM 1856 CA THR A 242 8.984 11.149 51.636 1.00 13.75 AATOM 1857 CB THR A 242 8.150 10.563 52.815 1.00 14.23 A ATOM 1858 OG1THR A 242 6.860 11.188 52.853 1.00 15.91 A ATOM 1859 CG2 THR A 242 8.86310.780 54.144 1.00 13.74 A ATOM 1860 C THR A 242 8.207 10.878 50.3501.00 13.35 A ATOM 1661 O THR A 242 7.526 11.757 49.820 1.00 13.22 A ATOM1862 N ALA A 243 8.310 9.648 49.856 1.00 12.74 A ATOM 1863 CA ALA A 2437.607 9.244 48.646 1.00 12.52 A ATOM 1864 CB ALA A 243 8.379 9.70247.410 1.00 12.73 A ATOM 1865 C ALA A 243 7.422 7.726 48.611 1.00 12.56A ATOM 1866 O ALA A 243 8.142 6.988 49.285 1.00 12.38 A ATOM 1867 N GLNA 244 6.430 7.276 47.848 1.00 12.33 A ATOM 1868 CA GLN A 244 6.158 5.85047.681 1.00 13.23 A ATOM 1869 CB GLN A 244 5.005 5.372 48.581 1.00 13.07A ATOM 1870 CG GLN A 244 4.761 3.860 48.475 1.00 12.26 A ATOM 1871 CDGLN A 244 3.457 3.383 49.114 1.00 12.34 A ATOM 1872 OE1 GLN A 244 2.3783.893 48.811 1.00 12.05 A ATOM 1873 NE2 GLN A 244 3.556 2.379 49.9891.00 10.52 A ATOM 1874 C GLN A 244 5.753 5.660 46.225 1.00 13.65 A ATOM1875 O GLN A 244 4.996 6.466 45.681 1.00 13.54 A ATOM 1876 N THR A 2456.260 4.611 45.588 1.00 14.00 A ATOM 1877 CA THR A 245 5.903 4.36144.200 1.00 14.97 A ATOM 1878 CB THR A 245 6.862 5.104 43.240 1.00 15.16A ATOM 1879 OG1 THR A 245 6.295 5.121 41.922 1.00 16.09 A ATOM 1880 CG2THR A 245 8.222 4.418 43.201 1.00 16.31 A ATOM 1881 C THR A 245 5.9082.872 43.875 1.00 15.50 A ATOM 1882 O THR A 245 6.472 2.069 44.616 1.0015.47 A ATOM 1883 N ILE A 246 5.257 2.516 42.770 1.00 16.25 A ATOM 1884CA ILE A 246 5.174 1.136 42.309 1.00 16.49 A ATOM 1885 CB ILE A 2463.698 0.719 42.056 1.00 16.23 A ATOM 1886 CG2 ILE A 246 3.636 −0.67941.456 1.00 15.84 A ATOM 1887 CG1 ILE A 246 2.915 0.748 43.376 1.0015.94 A ATOM 1888 CD1 ILE A 246 1.417 0.555 43.212 1.00 15.61 A ATOM1889 C ILE A 246 5.960 1.046 41.001 1.00 18.27 A ATOM 1890 O ILE A 2465.689 1.790 40.058 1.00 17.51 A ATOM 1891 N ALA A 247 6.937 0.145 40.9561.00 19.38 A ATOM 1892 CA ALA A 247 7.770 −0.025 39.768 1.00 21.64 AATOM 1893 CB ALA A 247 8.938 −0.960 40.080 1.00 21.46 A ATOM 1894 C ALAA 247 6.971 −0.566 38.584 1.00 23.14 A ATOM 1895 O ALA A 247 6.131−1.451 38.743 1.00 23.05 A ATOM 1896 N PRO A 248 7.223 −0.033 37.3781.00 24.93 A ATOM 1897 CD PRO A 248 8.193 1.027 37.042 1.00 25.33 A ATOM1898 CA PRO A 248 6.510 −0.488 36.183 1.00 26.41 A ATOM 1899 CB PRO A248 6.983 0.490 35.107 1.00 26.16 A ATOM 1900 CG PRO A 248 8.370 0.83435.554 1.00 26.28 A ATOM 1901 C PRO A 248 6.835 −1.945 35.847 1.00 28.02A ATOM 1902 O PRO A 248 7.964 −2.401 36.040 1.00 28.21 A ATOM 1903 N ASPA 249 5.832 −2.667 35.354 1.00 29.84 A ATOM 1904 CA ASP A 249 5.982−4.077 34.997 1.00 31.50 A ATOM 1905 CB ASP A 249 6.744 −4.214 33.6801.00 32.96 A ATOM 1906 CG ASP A 249 5.969 −3.663 32.506 1.00 34.22 AATOM 1907 OD1 ASP A 249 4.816 −4.104 32.299 1.00 35.29 A ATOM 1908 OD2ASP A 249 6.512 −2.794 31.792 1.00 35.24 A ATOM 1909 C ASP A 249 6.691−4.878 36.077 1.00 31.86 A ATOM 1910 O ASP A 249 7.796 −5.379 35.8671.00 32.42 A ATOM 1911 N SER A 250 6.049 −5.004 37.232 1.00 31.79 A ATOM1912 CA SER A 250 6.629 −5.747 38.338 1.00 31.71 A ATOM 1913 CB SER A250 7.363 −4.793 39.281 1.00 31.24 A ATOM 1914 OG SER A 250 6.458 −3.89039.883 1.00 30.46 A ATOM 1915 C SER A 250 5.556 −6.506 39.111 1.00 31.85A ATOM 1916 O SER A 250 5.839 −7.133 40.129 1.00 31.15 A ATOM 1917 N GLUA 251 4.321 −6.441 38.624 1.00 32.41 A ATOM 1918 CA GLU A 251 3.219−7.135 39.275 1.00 32.93 A ATOM 1919 CB GLU A 251 1.915 −6.885 38.5101.00 34.41 A ATOM 1920 CG GLU A 251 0.667 −7.443 39.186 1.00 36.20 AATOM 1921 CD GLU A 251 −0.612 −7.063 38.459 1.00 37.28 A ATOM 1922 OE1GLU A 251 −1.705 −7.458 38.925 1.00 37.89 A ATOM 1923 OE2 GLU A 251−0.525 −6.368 37.421 1.00 38.05 A ATOM 1924 C GLU A 251 3.542 −8.62539.301 1.00 32.68 A ATOM 1925 O GLU A 251 3.762 −9.240 38.254 1.00 32.66A ATOM 1926 N GLY A 252 3.595 −9.196 40.501 1.00 32.04 A ATOM 1927 CAGLY A 252 3.901 −10.609 40.637 1.00 30.95 A ATOM 1928 C GLY A 252 5.326−10.861 41.093 1.00 30.57 A ATOM 1929 O GLY A 252 5.672 −11.974 41.4881.00 30.50 A ATOM 1930 N ALA A 253 6.159 −9.827 41.045 1.00 29.95 A ATOM1931 CA ALA A 253 7.553 −9.955 41.454 1.00 29.30 A ATOM 1932 CB ALA A253 8.253 −8.608 41.344 1.00 29.04 A ATOM 1933 C ALA A 253 7.670 −10.49442.876 1.00 29.10 A ATOM 1934 O ALA A 253 8.502 −11.358 43.153 1.0028.97 A ATOM 1935 N ILE A 254 6.833 −9.977 43.772 1.00 29.05 A ATOM 1936CA ILE A 254 6.827 −10.404 45.169 1.00 28.75 A ATOM 1937 CB ILE A 2547.611 −9.424 46.070 1.00 28.87 A ATOM 1938 CG2 ILE A 254 7.593 −9.92247.511 1.00 29.14 A ATOM 1939 CG1 ILE A 254 9.055 −9.287 45.584 1.0029.03 A ATOM 1940 CD1 ILE A 254 9.901 −10.528 45.803 1.00 30.14 A ATOM1941 C ILE A 254 5.387 −10.447 45.670 1.00 28.64 A ATOM 1942 O ILE A 2544.730 −9.411 45.773 1.00 28.64 A ATOM 1943 N ASP A 255 4.895 −11.63945.989 1.00 28.26 A ATOM 1944 CA ASP A 255 3.525 −11.762 46.471 1.0027.70 A ATOM 1945 CB ASP A 255 2.598 −12.163 45.322 1.00 29.83 A ATOM1946 CG ASP A 255 2.660 −13.643 45.016 1.00 32.19 A ATOM 1947 OD1 ASP A255 2.153 −14.443 45.835 1.00 33.88 A ATOM 1948 OD2 ASP A 255 3.222−14.012 43.964 1.00 33.72 A ATOM 1949 C ASP A 255 3.401 −12.778 47.6001.00 26.17 A ATOM 1950 O ASP A 255 4.086 −13.803 47.612 1.00 26.56 AATOM 1951 N GLY A 256 2.519 −12.483 48.548 1.00 23.34 A ATOM 1952 CA GLYA 256 2.304 −13.379 49.664 1.00 20.65 A ATOM 1953 C GLY A 256 0.831−13.708 49.807 1.00 18.54 A ATOM 1954 O GLY A 256 −0.030 −12.931 49.3891.00 17.67 A ATOM 1955 N HIS A 257 0.537 −14.862 50.395 1.00 17.10 AATOM 1956 CA HIS A 257 −0.844 −15.289 50.586 1.00 16.09 A ATOM 1957 CBHIS A 257 −1.205 −16.374 49.567 1.00 17.01 A ATOM 1958 CG HIS A 257−0.976 −15.973 48.141 1.00 17.98 A ATOM 1959 CD2 HIS A 257 −0.126−16.458 47.204 1.00 18.47 A ATOM 1960 ND1 HIS A 257 −1.680 −14.95747.529 1.00 18.29 A ATOM 1961 CE1 HIS A 257 −1.275 −14.836 46.276 1.0018.53 A ATOM 1962 NE2 HIS A 257 −0.332 −15.734 46.054 1.00 18.65 A ATOM1963 C HIS A 257 −1.034 −15.842 51.997 1.00 15.08 A ATOM 1964 O HIS A257 −0.328 −16.771 52.400 1.00 14.51 A ATOM 1965 N LEU A 258 −1.981−15.274 52.744 1.00 13.67 A ATOM 1966 CA LEU A 258 −2.269 −15.735 54.1041.00 12.94 A ATOM 1967 CB LEU A 258 −2.743 −14.565 54.973 1.00 13.79 AATOM 1968 CG LEU A 258 −2.864 −14.775 56.490 1.00 14.04 A ATOM 1969 CD1LEU A 258 −3.994 −15.736 56.802 1.00 15.09 A ATOM 1970 CD2 LEU A 258−1.542 −15.300 57.035 1.00 13.98 A ATOM 1971 C LEU A 258 −3.369 −16.78953.972 1.00 12.65 A ATOM 1972 O LEU A 258 −4.527 −16.464 53.684 1.0011.92 A ATOM 1973 N ARG A 259 −2.998 −18.047 54.185 1.00 11.51 A ATOM1974 CA ARG A 259 −3.927 −19.162 54.033 1.00 12.09 A ATOM 1975 CB ARG A259 −3.614 −19.896 52.723 1.00 12.33 A ATOM 1976 CG ARG A 259 −3.690−19.023 51.473 1.00 12.60 A ATOM 1977 CD ARG A 259 −5.127 −18.640 51.1291.00 13.20 A ATOM 1978 NE ARG A 259 −5.220 −17.892 49.874 1.00 13.86 AATOM 1979 CZ ARG A 259 −5.066 −16.575 49.767 1.00 14.56 A ATOM 1980 NH1ARG A 259 −4.814 −15.846 50.843 1.00 13.37 A ATOM 1981 NH2 ARG A 259−5.163 −15.987 48.580 1.00 14.20 A ATOM 1982 C ARG A 259 −3.892 −20.15555.194 1.00 12.02 A ATOM 1983 O ARG A 259 −3.224 −19.925 56.208 1.0011.93 A ATOM 1984 N GLU A 260 −4.608 −21.266 55.032 1.00 12.07 A ATOM1985 CA GLU A 260 −4.677 −22.293 56.067 1.00 11.81 A ATOM 1986 CB GLU A260 −5.658 −23.401 55.638 1.00 12.66 A ATOM 1987 CG GLU A 260 −7.136−22.962 55.733 1.00 12.50 A ATOM 1988 CD GLU A 260 −8.119 −23.909 55.0371.00 13.49 A ATOM 1989 OE1 GLU A 260 −8.009 −25.138 55.209 1.00 13.25 AATOM 1990 OE2 GLU A 260 −9.020 −23.414 54.323 1.00 13.98 A ATOM 1991 CGLU A 260 −3.314 −22.877 56.433 1.00 12.29 A ATOM 1992 O GLU A 260−3.138 −23.412 57.531 1.00 12.18 A ATOM 1993 N ALA A 261 −2.344 −22.76055.530 1.00 12.23 A ATOM 1994 CA ALA A 261 −1.006 −23.282 55.789 1.0012.39 A ATOM 1995 CB ALA A 261 −0.454 −23.962 54.531 1.00 13.04 A ATOM1996 C ALA A 261 −0.047 −22.180 56.255 1.00 12.98 A ATOM 1997 O ALA A261 1.165 −22.383 56.308 1.00 12.59 A ATOM 1998 N GLY A 262 −0.591−21.016 56.596 1.00 13.18 A ATOM 1999 CA GLY A 262 0.249 −19.916 57.0331.00 13.93 A ATOM 2000 C GLY A 262 0.495 −18.934 55.902 1.00 14.52 AATOM 2001 O GLY A 262 −0.305 −18.850 54.965 1.00 14.28 A ATOM 2002 N LEUA 263 1.598 −18.193 55.981 1.00 15.26 A ATOM 2003 CA LEU A 263 1.944−17.210 54.954 1.00 16.05 A ATOM 2004 CB LEU A 263 2.466 −15.924 55.6091.00 15.77 A ATOM 2005 CG LEU A 263 2.933 −14.826 54.646 1.00 15.80 AATOM 2006 CD1 LEU A 263 1.737 −14.294 53.861 1.00 16.55 A ATOM 2007 CD2LEU A 263 3.604 −13.700 55.424 1.00 15.82 A ATOM 2008 C LEU A 263 2.997−17.737 53.976 1.00 17.41 A ATOM 2009 O LEU A 263 4.087 −18.131 54.3881.00 15.70 A ATOM 2010 N THR A 264 2.669 −17.745 52.683 1.00 19.51 AATOM 2011 CA THR A 264 3.604 −18.203 51.652 1.00 22.55 A ATOM 2012 CBTHR A 264 3.032 −19.396 50.841 1.00 22.62 A ATOM 2013 OG1 THR A 2641.814 −19.005 50.193 1.00 22.53 A ATOM 2014 CG2 THR A 264 2.758 −20.57851.759 1.00 22.97 A ATOM 2015 C THR A 264 3.930 −17.061 50.684 1.0025.08 A ATOM 2016 O THR A 264 3.152 −16.116 50.553 1.00 24.86 A ATOM2017 N PHE A 265 5.080 −17.150 50.014 1.00 27.68 A ATOM 2018 CA PHE A265 5.520 −16.124 49.059 1.00 30.90 A ATOM 2019 CB PHE A 265 6.761−15.399 49.590 1.00 31.48 A ATOM 2020 CG PHE A 265 6.458 −14.282 50.5501.00 31.83 A ATOM 2021 CD1 PHE A 265 5.800 −13.133 50.116 1.00 32.13 AATOM 2022 CD2 PHE A 265 6.851 −14.364 51.882 1.00 31.97 A ATOM 2023 CE1PHE A 265 5.541 −12.080 50.997 1.00 31.84 A ATOM 2024 CE2 PHE A 2656.595 −13.316 52.770 1.00 32.16 A ATOM 2025 CZ PHE A 265 5.941 −12.17452.325 1.00 31.81 A ATOM 2026 C PHE A 265 5.844 −16.701 47.679 1.0033.06 A ATOM 2027 O PHE A 265 6.356 −17.817 47.572 1.00 33.32 A ATOM2028 N HIS A 266 5.552 −15.931 46.630 1.00 35.28 A ATOM 2029 CA HIS A266 5.803 −16.354 45.249 1.00 37.58 A ATOM 2030 CB HIS A 266 4.495−16.800 44.589 1.00 38.61 A ATOM 2031 CG HIS A 266 3.760 −17.857 45.3551.00 40.09 A ATOM 2032 CD2 HIS A 266 3.407 −19.120 45.018 1.00 40.75 AATOM 2033 ND1 HIS A 266 3.288 −17.657 46.635 1.00 40.98 A ATOM 2034 CE1HIS A 266 2.674 −18.750 47.053 1.00 41.00 A ATOM 2035 NE2 HIS A 2662.732 −19.653 46.090 1.00 41.36 A ATOM 2036 C HIS A 266 6.427 −15.22444.421 1.00 38.52 A ATOM 2037 O HIS A 266 5.931 −14.096 44.426 1.0038.95 A ATOM 2038 N LEU A 267 7.503 −15.533 43.699 1.00 39.31 A ATOM2039 CA LEU A 267 8.197 −14.531 42.889 1.00 39.61 A ATOM 2040 CB LEU A267 9.705 −14.576 43.174 1.00 39.95 A ATOM 2041 CG LEU A 267 10.194−14.308 44.603 1.00 40.58 A ATOM 2042 CD1 LEU A 267 9.725 −15.410 45.5411.00 40.74 A ATOM 2043 CD2 LEU A 267 11.711 −14.243 44.608 1.00 40.64 AATOM 2044 C LEU A 267 7.975 −14.660 41.381 1.00 39.65 A ATOM 2045 O LEUA 267 7.598 −15.719 40.878 1.00 39.80 A ATOM 2046 N ALA A 268 8.217−13.562 40.670 1.00 39.52 A ATOM 2047 CA ALA A 268 8.069 −13.510 39.2181.00 39.27 A ATOM 2048 CB ALA A 268 6.646 −13.114 38.846 1.00 39.26 AATOM 2049 C ALA A 268 9.062 −12.486 38.673 1.00 39.03 A ATOM 2050 O ALAA 268 8.990 −11.303 39.004 1.00 39.11 A ATOM 2051 N GLY A 269 9.988−12.942 37.837 1.00 38.84 A ATOM 2052 CA GLY A 269 10.985 −12.040 37.2881.00 38.15 A ATOM 2053 C GLY A 269 12.158 −11.931 38.247 1.00 37.50 AATOM 2054 O GLY A 269 12.241 −12.699 39.206 1.00 37.96 A ATOM 2055 N ALAA 270 13.058 −10.983 38.003 1.00 36.27 A ATOM 2056 CA ALA A 270 14.223−10.808 38.865 1.00 34.83 A ATOM 2057 CB ALA A 270 15.486 −10.771 38.0191.00 35.40 A ATOM 2058 C ALA A 270 14.130 −9.547 39.724 1.00 33.76 AATOM 2059 O ALA A 270 14.279 −8.431 39.224 1.00 33.47 A ATOM 2060 N VALA 271 13.892 −9.737 41.019 1.00 32.23 A ATOM 2061 CA VAL A 271 13.773−8.626 41.961 1.00 31.04 A ATOM 2062 CB VAL A 271 13.521 −9.145 43.4021.00 31.01 A ATOM 2063 CG1 VAL A 271 13.626 −8.003 44.404 1.00 30.77 AATOM 2064 CG2 VAL A 271 12.151 −9.783 43.484 1.00 31.12 A ATOM 2065 CVAL A 271 14.989 −7.697 41.972 1.00 29.97 A ATOM 2066 O VAL A 271 14.841−6.479 41.883 1.00 30.03 A ATOM 2067 N PRO A 272 16.206 −8.256 42.0861.00 29.22 A ATOM 2068 CD PRO A 272 16.559 −9.677 42.254 1.00 28.94 AATOM 2069 CA PRO A 272 17.410 −7.417 42.104 1.00 28.46 A ATOM 2070 CBPRO A 272 18.542 −8.442 42.131 1.00 28.41 A ATOM 2071 CG PRO A 27217.932 −9.590 42.878 1.00 28.73 A ATOM 2072 C PRO A 272 17.509 −6.47940.897 1.00 27.94 A ATOM 2073 O PRO A 272 17.907 −5.323 41.032 1.0027.50 A ATOM 2074 N ASP A 273 17.147 −6.986 39.722 1.00 27.25 A ATOM2075 CA ASP A 273 17.193 −6.196 38.496 1.00 26.96 A ATOM 2076 CB ASP A273 16.970 −7.099 37.281 1.00 27.99 A ATOM 2077 CG ASP A 273 18.228−7.831 36.859 1.00 29.35 A ATOM 2078 OD1 ASP A 273 18.956 −8.347 37.7341.00 30.19 A ATOM 2079 OD2 ASP A 273 18.488 −7.899 35.642 1.00 31.21 AATOM 2080 C ASP A 273 16.164 −5.070 38.494 1.00 26.29 A ATOM 2081 O ASPA 273 16.457 −3.951 38.082 1.00 25.72 A ATOM 2082 N ILE A 274 14.954−5.368 38.952 1.00 26.11 A ATOM 2083 CA ILE A 274 13.899 −4.363 38.9901.00 25.68 A ATOM 2084 CB ILE A 274 12.561 −4.987 39.440 1.00 25.78 AATOM 2085 CG2 ILE A 274 11.480 −3.915 39.498 1.00 25.49 A ATOM 2086 CG1ILE A 274 12.169 −6.103 38.465 1.00 26.11 A ATOM 2087 CD1 ILE A 27410.946 −6.901 38.866 1.00 26.62 A ATOM 2088 C ILE A 274 14.281 −3.21539.925 1.00 25.55 A ATOM 2089 O ILE A 274 14.087 −2.045 39.594 1.0024.97 A ATOM 2090 N VAL A 275 14.838 −3.550 41.086 1.00 25.89 A ATOM2091 CA VAL A 275 15.249 −2.530 42.048 1.00 26.31 A ATOM 2092 CB VAL A275 15.736 −3.164 43.380 1.00 26.56 A ATOM 2093 CG1 VAL A 275 16.295−2.087 44.301 1.00 26.70 A ATOM 2094 CG2 VAL A 275 14.586 −3.886 44.0681.00 26.15 A ATOM 2095 C VAL A 275 16.371 −1.657 41.482 1.00 26.97 AATOM 2096 O VAL A 275 16.257 −0.433 41.458 1.00 27.12 A ATOM 2097 N SERA 276 17.442 −2.289 41.006 1.00 27.37 A ATOM 2098 CA SER A 276 18.587−1.559 40.465 1.00 28.02 A ATOM 2099 CB SER A 276 19.741 −2.526 40.1731.00 28.39 A ATOM 2100 OG SER A 276 19.374 −3.502 39.214 1.00 28.82 AATOM 2101 C SER A 276 18.286 −0.729 39.218 1.00 28.31 A ATOM 2102 O SERA 276 18.977 0.254 38.947 1.00 28.51 A ATOM 2103 N LYS A 277 17.265−1.116 38.461 1.00 28.38 A ATOM 2104 CA LYS A 277 16.901 −0.379 37.2551.00 28.77 A ATOM 2105 CB LYS A 277 16.196 −1.298 36.255 1.00 30.10 AATOM 2106 CG LYS A 277 17.077 −2.408 35.702 1.00 32.06 A ATOM 2107 CDLYS A 277 16.333 −3.237 34.667 1.00 33.51 A ATOM 2108 CE LYS A 27717.151 −4.443 34.229 1.00 34.41 A ATOM 2109 NZ LYS A 277 18.471 −4.06033.652 1.00 34.50 A ATOM 2110 C LYS A 277 15.998 0.814 37.556 1.00 28.23A ATOM 2111 O LYS A 277 15.910 1.745 36.756 1.00 28.03 A ATOM 2112 N ASNA 278 15.339 0.784 38.712 1.00 27.01 A ATOM 2113 CA ASN A 278 14.4271.853 39.115 1.00 26.27 A ATOM 2114 CB ASN A 278 13.103 1.253 39.5911.00 26.13 A ATOM 2115 CG ASN A 278 12.247 0.739 38.447 1.00 26.09 AATOM 2116 OD1 ASN A 278 11.588 1.516 37.752 1.00 26.66 A ATOM 2117 ND2ASN A 278 12.261 −0.572 38.240 1.00 25.15 A ATOM 2118 C ASN A 278 14.9892.735 40.221 1.00 26.25 A ATOM 2119 O ASN A 278 14.376 3.738 40.591 1.0026.18 A ATOM 2120 N ILE A 279 16.155 2.370 40.743 1.00 25.52 A ATOM 2121CA ILE A 279 16.762 3.123 41.830 1.00 25.04 A ATOM 2122 CB ILE A 27917.921 2.327 42.474 1.00 25.04 A ATOM 2123 CG2 ILE A 279 19.131 2.29941.548 1.00 25.43 A ATOM 2124 CG1 ILE A 279 18.284 2.951 43.820 1.0024.74 A ATOM 2125 CD1 ILE A 279 17.153 2.907 44.818 1.00 24.79 A ATOM2126 C ILE A 279 17.265 4.513 41.446 1.00 24.99 A ATOM 2127 O ILE A 27917.085 5.468 42.204 1.00 24.98 A ATOM 2128 N THR A 280 17.887 4.63640.276 1.00 24.16 A ATOM 2129 CA THR A 280 18.406 5.927 39.846 1.0023.97 A ATOM 2130 CB THR A 280 19.122 5.831 38.480 1.00 23.59 A ATOM2131 OG1 THR A 280 20.213 4.907 38.573 1.00 23.27 A ATOM 2132 CG2 THR A280 19.661 7.195 38.069 1.00 23.09 A ATOM 2133 C THR A 280 17.309 6.97839.745 1.00 24.11 A ATOM 2134 O THR A 280 17.489 8.109 40.197 1.00 23.96A ATOM 2135 N LYS A 281 16.172 6.608 39.161 1.00 24.39 A ATOM 2136 CALYS A 281 15.069 7.550 39.010 1.00 24.90 A ATOM 2137 CB LYS A 281 13.9626.949 38.140 1.00 26.58 A ATOM 2138 CG LYS A 281 13.414 5.626 38.6311.00 28.54 A ATOM 2139 CD LYS A 281 12.272 5.129 37.750 1.00 30.15 AATOM 2140 CE LYS A 281 11.047 6.036 37.837 1.00 31.02 A ATOM 2141 NZ LYSA 281 11.308 7.427 37.359 1.00 32.08 A ATOM 2142 C LYS A 281 14.5017.990 40.353 1.00 24.09 A ATOM 2143 O LYS A 281 14.058 9.128 40.502 1.0024.02 A ATOM 2144 N ALA A 282 14.509 7.092 41.331 1.00 23.31 A ATOM 2145CA ALA A 282 14.004 7.434 42.658 1.00 22.44 A ATOM 2146 CB ALA A 28213.877 6.176 43.517 1.00 22.10 A ATOM 2147 C ALA A 282 14.967 8.43243.309 1.00 22.14 A ATOM 2148 O ALA A 282 14.544 9.360 43.999 1.00 21.76A ATOM 2149 N LEU A 283 16.264 8.240 43.074 1.00 21.91 A ATOM 2150 CALEU A 283 17.298 9.119 43.627 1.00 22.25 A ATOM 2151 CB LEU A 283 18.6818.487 43.466 1.00 21.95 A ATOM 2152 CG LEU A 283 19.137 7.434 44.4711.00 21.65 A ATOM 2153 CD1 LEU A 283 20.407 6.781 43.954 1.00 21.52 AATOM 2154 CD2 LEU A 283 19.372 8.078 45.837 1.00 20.87 A ATOM 2155 C LEUA 283 17.324 10.498 42.977 1.00 22.77 A ATOM 2156 O LEU A 283 17.44811.513 43.667 1.00 22.46 A ATOM 2157 N VAL A 284 17.235 10.535 41.6511.00 23.26 A ATOM 2158 CA VAL A 284 17.258 11.810 40.942 1.00 24.56 AATOM 2159 CB VAL A 284 17.197 11.617 39.402 1.00 24.60 A ATOM 2160 CG1VAL A 284 18.434 10.888 38.922 1.00 24.22 A ATOM 2161 CG2 VAL A 28415.948 10.847 39.018 1.00 25.47 A ATOM 2162 C VAL A 284 16.099 12.69641.371 1.00 25.10 A ATOM 2163 O VAL A 284 16.268 13.896 41.576 1.0026.07 A ATOM 2164 N GLU A 285 14.924 12.097 41.520 1.00 25.93 A ATOM2165 CA GLU A 285 13.732 12.832 41.915 1.00 26.80 A ATOM 2166 CB GLU A285 12.500 11.947 41.715 1.00 28.36 A ATOM 2167 CG GLU A 285 11.24112.450 42.384 1.00 31.15 A ATOM 2168 CD GLU A 285 10.001 11.815 41.8091.00 32.58 A ATOM 2169 OE1 GLU A 285 10.025 10.588 41.569 1.00 34.38 AATOM 2170 OE2 GLU A 285 9.000 12.538 41.599 1.00 34.22 A ATOM 2171 C GLUA 285 13.788 13.347 43.351 1.00 26.74 A ATOM 2172 O GLU A 285 13.17414.363 43.676 1.00 26.52 A ATOM 2173 N ALA A 286 14.534 12.655 44.2051.00 26.28 A ATOM 2174 CA ALA A 286 14.651 13.057 45.602 1.00 26.53 AATOM 2175 CB ALA A 286 14.821 11.821 46.477 1.00 25.97 A ATOM 2176 C ALAA 286 15.797 14.035 45.864 1.00 26.80 A ATOM 2177 O ALA A 286 15.68314.921 46.713 1.00 26.76 A ATOM 2178 N PHE A 287 16.894 13.884 45.1271.00 27.08 A ATOM 2179 CA PHE A 287 18.062 14.733 45.329 1.00 27.56 AATOM 2180 CB PHE A 287 19.294 13.848 45.536 1.00 26.16 A ATOM 2181 CGPHE A 287 19.300 13.142 46.860 1.00 25.16 A ATOM 2182 CD1 PHE A 28719.599 13.837 48.027 1.00 24.31 A ATOM 2183 CD2 PHE A 287 18.941 11.80246.952 1.00 24.68 A ATOM 2184 CE1 PHE A 287 19.538 13.210 49.270 1.0024.57 A ATOM 2185 CE2 PHE A 287 18.876 11.164 48.191 1.00 24.72 A ATOM2186 CZ PHE A 287 19.174 11.872 49.353 1.00 24.05 A ATOM 2187 C PHE A287 18.354 15.805 44.282 1.00 29.00 A ATOM 2188 O PHE A 287 19.23116.646 44.487 1.00 28.79 A ATOM 2189 N GLU A 288 17.636 15.781 43.1641.00 30.59 A ATOM 2190 CA GLU A 288 17.845 16.801 42.138 1.00 32.44 AATOM 2191 CB GLU A 288 16.899 16.581 40.954 1.00 33.45 A ATOM 2192 CGGLU A 288 17.114 17.546 39.799 1.00 35.64 A ATOM 2193 CD GLU A 28816.158 17.296 38.646 1.00 36.73 A ATOM 2194 OE1 GLU A 288 14.950 17.57738.796 1.00 37.57 A ATOM 2195 OE2 GLU A 288 16.616 16.808 37.592 1.0037.77 A ATOM 2196 C GLU A 288 17.588 18.176 42.761 1.00 32.65 A ATOM2197 O GLU A 288 18.391 19.095 42.608 1.00 33.11 A ATOM 2198 N PRO A 28916.463 18.329 43.482 1.00 33.05 A ATOM 2199 CD PRO A 289 15.364 17.35843.650 1.00 33.26 A ATOM 2200 CA PRO A 289 16.121 19.602 44.125 1.0033.05 A ATOM 2201 CB PRO A 289 14.818 19.279 44.851 1.00 33.14 A ATOM2202 CG PRO A 289 14.192 18.256 43.966 1.00 33.18 A ATOM 2203 C PRO A289 17.196 20.118 45.083 1.00 33.10 A ATOM 2204 O PRO A 289 17.29821.324 45.315 1.00 33.32 A ATOM 2205 N LEU A 290 17.988 19.206 45.6411.00 32.89 A ATOM 2206 CA LEU A 290 19.047 19.580 46.577 1.00 32.40 AATOM 2207 CB LEU A 290 19.289 18.457 47.596 1.00 32.52 A ATOM 2208 CGLEU A 290 18.136 18.060 48.524 1.00 32.73 A ATOM 2209 CD1 LEU A 29018.595 16.961 49.469 1.00 32.65 A ATOM 2210 CD2 LEU A 290 17.672 19.26749.313 1.00 32.85 A ATOM 2211 C LEU A 290 20.351 19.887 45.852 1.0032.01 A ATOM 2212 O LEU A 290 21.323 20.330 46.468 1.00 31.92 A ATOM2213 N GLY A 291 20.369 19.640 44.545 1.00 31.46 A ATOM 2214 CA GLY A291 21.559 19.898 43.753 1.00 30.99 A ATOM 2215 C GLY A 291 22.66318.874 43.948 1.00 30.50 A ATOM 2216 O GLY A 291 23.839 19.169 43.7261.00 30.55 A ATOM 2217 N ILE A 292 22.290 17.665 44.355 1.00 29.69 AATOM 2218 CA ILE A 292 23.261 16.601 44.583 1.00 29.08 A ATOM 2219 CBILE A 292 23.031 15.937 45.953 1.00 29.06 A ATOM 2220 CG2 ILE A 29223.989 14.764 46.135 1.00 28.81 A ATOM 2221 CG1 ILE A 292 23.224 16.97347.066 1.00 28.76 A ATOM 2222 CD1 ILE A 292 22.920 16.455 48.454 1.0028.39 A ATOM 2223 C ILE A 292 23.189 15.530 43.499 1.00 28.90 A ATOM2224 O ILE A 292 22.140 14.926 43.282 1.00 28.79 A ATOM 2225 N SER A 29324.312 15.302 42.821 1.00 28.59 A ATOM 2226 CA SER A 293 24.381 14.30441.756 1.00 28.30 A ATOM 2227 CB SER A 293 24.792 14.969 40.440 1.0028.20 A ATOM 2228 OG SER A 293 26.091 15.529 40.548 1.00 28.70 A ATOM2229 C SER A 293 25.373 13.188 42.087 1.00 27.62 A ATOM 2230 O SER A 29325.332 12.119 41.485 1.00 27.89 A ATOM 2231 N ASP A 294 26.265 13.44643.039 1.00 27.00 A ATOM 2232 CA ASP A 294 27.266 12.463 43.450 1.0026.30 A ATOM 2233 CB ASP A 294 28.587 13.173 43.769 1.00 27.80 A ATOM2234 CG ASP A 294 29.621 12.246 44.379 1.00 28.79 A ATOM 2235 OD1 ASP A294 29.606 11.037 44.063 1.00 28.85 A ATOM 2236 OD2 ASP A 294 30.45912.735 45.168 1.00 30.27 A ATOM 2237 C ASP A 294 26.770 11.676 44.6671.00 25.13 A ATOM 2238 O ASP A 294 26.850 12.151 45.797 1.00 24.51 AATOM 2239 N TYR A 295 26.276 10.465 44.424 1.00 23.98 A ATOM 2240 CA TYRA 295 25.727 9.628 45.487 1.00 22.92 A ATOM 2241 CB TYR A 295 24.9018.504 44.861 1.00 23.20 A ATOM 2242 CG TYR A 295 23.850 9.050 43.9221.00 23.56 A ATOM 2243 CD1 TYR A 295 22.910 9.985 44.366 1.00 24.31 AATOM 2244 CE1 TYR A 295 21.984 10.552 43.491 1.00 24.25 A ATOM 2245 CD2TYR A 295 23.833 8.690 42.573 1.00 24.63 A ATOM 2246 CE2 TYR A 29522.911 9.251 41.688 1.00 24.54 A ATOM 2247 CZ TYR A 295 21.992 10.18242.153 1.00 24.93 A ATOM 2248 OH TYR A 295 21.095 10.752 41.279 1.0024.87 A ATOM 2249 C TYR A 295 26.723 9.088 46.514 1.00 22.33 A ATOM 2250O TYR A 295 26.338 8.392 47.455 1.00 21.89 A ATOM 2251 N ASN A 29628.001 9.407 46.339 1.00 21.23 A ATOM 2252 CA ASN A 296 29.011 8.99947.306 1.00 20.36 A ATOM 2253 CB ASN A 296 30.383 8.844 46.641 1.0021.14 A ATOM 2254 CG ASN A 296 30.596 7.460 46.052 1.00 20.97 A ATOM2255 OD1 ASN A 296 30.624 6.464 46.776 1.00 21.95 A ATOM 2256 ND2 ASN A296 30.749 7.392 44.735 1.00 20.64 A ATOM 2257 C ASN A 296 29.073 10.10448.359 1.00 19.68 A ATOM 2258 O ASN A 296 29.722 9.959 49.395 1.00 19.26A ATOM 2259 N SER A 297 28.373 11.206 48.089 1.00 19.05 A ATOM 2260 CASER A 297 28.354 12.345 49.003 1.00 18.66 A ATOM 2261 CB SER A 29728.379 13.659 48.209 1.00 18.96 A ATOM 2262 OG SER A 297 27.200 13.83347.438 1.00 20.75 A ATOM 2263 C SER A 297 27.196 12.379 50.006 1.0018.07 A ATOM 2264 O SER A 297 26.998 13.387 50.687 1.00 17.98 A ATOM2265 N ILE A 298 26.435 11.292 50.101 1.00 17.31 A ATOM 2266 CA ILE A298 25.312 11.216 51.046 1.00 16.71 A ATOM 2267 CB ILE A 298 23.94911.279 50.305 1.00 16.38 A ATOM 2268 CG2 ILE A 298 23.849 12.575 49.5041.00 16.94 A ATOM 2269 CG1 ILE A 298 23.797 10.070 49.375 1.00 16.73 AATOM 2270 CD1 ILE A 298 22.459 10.005 48.652 1.00 16.32 A ATOM 2271 CILE A 298 25.392 9.891 51.814 1.00 16.04 A ATOM 2272 O ILE A 298 26.0068.943 51.317 1.00 16.33 A ATOM 2273 N PHE A 299 24.810 9.819 53.018 1.0015.01 A ATOM 2274 CA PHE A 299 24.843 8.556 53.759 1.00 14.11 A ATOM2275 CB PHE A 299 24.851 8.754 55.292 1.00 13.75 A ATOM 2276 CG PHE A299 23.689 9.547 55.850 1.00 12.78 A ATOM 2277 CD1 PHE A 299 23.71310.939 55.852 1.00 12.57 A ATOM 2278 CD2 PHE A 299 22.616 8.897 56.4551.00 12.47 A ATOM 2279 CE1 PHE A 299 22.687 11.674 56.458 1.00 12.78 AATOM 2280 CE2 PHE A 299 21.583 9.620 57.064 1.00 12.49 A ATOM 2281 CZPHE A 299 21.620 11.012 57.066 1.00 12.45 A ATOM 2282 C PHE A 299 23.6987.645 53.311 1.00 14.17 A ATOM 2283 O PHE A 299 22.620 8.119 52.932 1.0014.13 A ATOM 2284 N TRP A 300 23.953 6.338 53.347 1.00 13.43 A ATOM 2285CA TRP A 300 23.012 5.330 52.863 1.00 13.55 A ATOM 2286 CB TRP A 30023.689 4.499 51.756 1.00 13.64 A ATOM 2287 CG TRP A 300 23.741 5.12850.398 1.00 14.19 A ATOM 2288 CD2 TRP A 300 22.917 4.794 49.275 1.0014.07 A ATOM 2289 CE2 TRP A 300 23.295 5.642 48.212 1.00 14.33 A ATOM2290 CE3 TRP A 300 21.888 3.861 49.067 1.00 14.36 A ATOM 2291 CD1 TRP A300 24.568 6.134 49.981 1.00 14.12 A ATOM 2292 NE1 TRP A 300 24.3056.447 48.669 1.00 14.30 A ATOM 2293 CZ2 TRP A 300 22.683 5.585 46.9531.00 14.52 A ATOM 2294 CZ3 TRP A 300 21.278 3.805 47.813 1.00 14.75 AATOM 2295 CH2 TRP A 300 21.679 4.665 46.774 1.00 14.61 A ATOM 2296 C TRPA 300 22.394 4.327 53.840 1.00 12.97 A ATOM 2297 O TRP A 300 23.0673.808 54.733 1.00 13.38 A ATOM 2298 N ILE A 301 21.109 4.050 53.631 1.0012.82 A ATOM 2299 CA ILE A 301 20.370 3.041 54.389 1.00 12.85 A ATOM2300 CB ILE A 301 19.465 3.629 55.510 1.00 12.55 A ATOM 2301 CG2 ILE A301 18.614 2.508 56.122 1.00 12.29 A ATOM 2302 CG1 ILE A 301 20.3114.266 56.620 1.00 12.45 A ATOM 2303 CD1 ILE A 301 20.591 5.741 56.4121.00 11.84 A ATOM 2304 C ILE A 301 19.471 2.341 53.356 1.00 13.12 A ATOM2305 O ILE A 301 18.549 2.951 52.806 1.00 13.40 A ATOM 2306 N ALA A 30219.754 1.072 53.073 1.00 13.05 A ATOM 2307 CA ALA A 302 18.965 0.32152.093 1.00 13.27 A ATOM 2308 CB ALA A 302 19.806 0.064 50.836 1.0013.42 A ATOM 2309 C ALA A 302 18.462 −1.006 52.658 1.00 13.08 A ATOM2310 O ALA A 302 19.217 −1.741 53.295 1.00 13.86 A ATOM 2311 N HIS A 30317.188 −1.313 52.425 1.00 12.38 A ATOM 2312 CA HIS A 303 16.613 −2.56652.905 1.00 12.20 A ATOM 2313 CB HIS A 303 15.131 −2.673 52.516 1.0011.11 A ATOM 2314 CG HIS A 303 14.535 −4.016 52.809 1.00 10.71 A ATOM2315 CD2 HIS A 303 14.074 −4.986 51.983 1.00 10.88 A ATOM 2316 ND1 HIS A303 14.422 −4.518 54.088 1.00 11.15 A ATOM 2317 CE1 HIS A 303 13.918−5.739 54.039 1.00 10.53 A ATOM 2318 NE2 HIS A 303 13.699 −6.047 52.7731.00 10.34 A ATOM 2319 C HIS A 303 17.390 −3.732 52.295 1.00 12.67 AATOM 2320 O HIS A 303 17.415 −3.901 51.076 1.00 12.89 A ATOM 2321 N PROA 304 18.033 −4.558 53.137 1.00 13.61 A ATOM 2322 CD PRO A 304 18.161−4.439 54.602 1.00 14.16 A ATOM 2323 CA PRO A 304 18.808 −5.698 52.6381.00 14.34 A ATOM 2324 CB PRO A 304 19.786 −5.950 53.774 1.00 14.36 AATOM 2325 CG PRO A 304 18.916 −5.711 54.973 1.00 14.60 A ATOM 2326 C PROA 304 17.956 −6.929 52.324 1.00 14.55 A ATOM 2327 O PRO A 304 18.096−7.965 52.972 1.00 15.04 A ATOM 2328 N GLY A 305 17.077 −6.809 51.3311.00 14.61 A ATOM 2329 CA GLY A 305 16.224 −7.925 50.966 1.00 14.76 AATOM 2330 C GLY A 305 17.055 −9.156 50.666 1.00 15.27 A ATOM 2331 O GLYA 305 16.671 −10.275 51.006 1.00 15.14 A ATOM 2332 N GLY A 306 18.199−8.938 50.027 1.00 15.34 A ATOM 2333 CA GLY A 306 19.102 −10.025 49.6781.00 16.49 A ATOM 2334 C GLY A 306 20.457 −9.455 49.307 1.00 16.93 AATOM 2335 O GLY A 306 20.564 −8.249 49.082 1.00 17.30 A ATOM 2336 N PROA 307 21.515 −10.278 49.228 1.00 17.46 A ATOM 2337 CD PRO A 307 21.579−11.730 49.472 1.00 18.01 A ATOM 2338 CA PRO A 307 22.836 −9.748 48.8741.00 18.03 A ATOM 2339 CB PRO A 307 23.761 −10.938 49.126 1.00 18.12 AATOM 2340 CG PRO A 307 22.891 −12.109 48.814 1.00 18.51 A ATOM 2341 CPRO A 307 22.949 −9.212 47.444 1.00 18.05 A ATOM 2342 O PRO A 307 23.710−8.272 47.184 1.00 17.85 A ATOM 2343 N ALA A 308 22.191 −9.803 46.5241.00 17.71 A ATOM 2344 CA ALA A 308 22.224 −9.383 45.126 1.00 18.01 AATOM 2345 CB ALA A 308 21.413 −10.347 44.269 1.00 18.21 A ATOM 2346 CALA A 308 21.715 −7.956 44.926 1.00 18.23 A ATOM 2347 O ALA A 308 22.236−7.219 44.085 1.00 18.16 A ATOM 2348 N ILE A 309 20.691 −7.569 45.6811.00 17.84 A ATOM 2349 CA ILE A 309 20.155 −6.217 45.561 1.00 17.99 AATOM 2350 CB ILE A 309 18.928 −6.011 46.480 1.00 18.26 A ATOM 2351 CG2ILE A 309 18.527 −4.541 46.488 1.00 18.23 A ATOM 2352 CG1 ILE A 30917.771 −6.893 45.999 1.00 18.73 A ATOM 2353 CD1 ILE A 309 16.508 −6.78546.833 1.00 19.58 A ATOM 2354 C ILE A 309 21.238 −5.204 45.925 1.0017.80 A ATOM 2355 O ILE A 309 21.412 −4.191 45.243 1.00 17.95 A ATOM2356 N LEU A 310 21.978 −5.488 46.992 1.00 17.66 A ATOM 2357 CA LEU A310 23.051 −4.600 47.428 1.00 17.75 A ATOM 2358 CB LEU A 310 23.611−5.070 48.774 1.00 17.50 A ATOM 2359 CG LEU A 310 22.609 −5.217 49.9261.00 17.03 A ATOM 2360 CD1 LEU A 310 23.348 −5.610 51.199 1.00 16.69 AATOM 2361 CD2 LEU A 310 21.863 −3.908 50.138 1.00 17.12 A ATOM 2362 CLEU A 310 24.182 −4.513 46.392 1.00 18.34 A ATOM 2363 O LEU A 310 24.685−3.422 46.102 1.00 17.54 A ATOM 2364 N ASP A 311 24.578 −5.655 45.8321.00 18.40 A ATOM 2365 CA ASP A 311 25.645 −5.673 44.829 1.00 19.39 AATOM 2366 CB ASP A 311 25.973 −7.107 44.384 1.00 19.51 A ATOM 2367 CGASP A 311 26.604 −7.945 45.483 1.00 20.61 A ATOM 2368 OD1 ASP A 31127.210 −7.374 46.416 1.00 20.57 A ATOM 2369 OD2 ASP A 311 26.509 −9.18945.395 1.00 21.12 A ATOM 2370 C ASP A 311 25.273 −4.860 43.588 1.0019.57 A ATOM 2371 O ASP A 311 26.079 −4.072 43.090 1.00 19.38 A ATOM2372 N GLN A 312 24.057 −5.059 43.086 1.00 20.06 A ATOM 2373 CA GLN A312 23.604 −4.351 41.890 1.00 20.92 A ATOM 2374 CB GLN A 312 22.336−5.011 41.331 1.00 21.67 A ATOM 2375 CG GLN A 312 22.644 −6.263 40.5111.00 22.92 A ATOM 2376 CD GLN A 312 21.408 −6.980 40.001 1.00 23.83 AATOM 2377 OE1 GLN A 312 20.503 −6.365 39.435 1.00 24.46 A ATOM 2378 NE2GLN A 312 21.372 −8.297 40.187 1.00 24.27 A ATOM 2379 C GLN A 312 23.389−2.856 42.106 1.00 21.43 A ATOM 2380 O GLN A 312 23.610 −2.054 41.1931.00 21.12 A ATOM 2381 N VAL A 313 22.964 −2.472 43.304 1.00 21.36 AATOM 2382 CA VAL A 313 22.772 −1.056 43.593 1.00 22.26 A ATOM 2383 CBVAL A 313 22.064 −0.847 44.958 1.00 21.61 A ATOM 2384 CG1 VAL A 31322.126 0.618 45.368 1.00 21.70 A ATOM 2385 CG2 VAL A 313 20.610 −1.28044.856 1.00 21.27 A ATOM 2386 C VAL A 313 24.152 −0.399 43.620 1.0022.76 A ATOM 2387 O VAL A 313 24.365 0.652 43.016 1.00 22.83 A ATOM 2388N GLU A 314 25.090 −1.044 44.306 1.00 23.89 A ATOM 2389 CA GLU A 31426.452 −0.539 44.423 1.00 24.82 A ATOM 2390 CB GLU A 314 27.285 −1.49045.290 1.00 26.33 A ATOM 2391 CG GLU A 314 28.633 −0.930 45.720 1.0028.97 A ATOM 2392 CD GLU A 314 29.345 −1.809 46.737 1.00 30.11 A ATOM2393 OE1 GLU A 314 28.730 −2.158 47.768 1.00 30.61 A ATOM 2394 OE2 GLU A314 30.528 −2.141 46.511 1.00 31.99 A ATOM 2395 C GLU A 314 27.107−0.370 43.046 1.00 25.07 A ATOM 2396 O GLU A 314 27.788 0.627 42.7901.00 24.35 A ATOM 2397 N GLN A 315 26.893 −1.339 42.162 1.00 24.83 AATOM 2398 CA GLN A 315 27.472 −1.280 40.823 1.00 25.91 A ATOM 2399 CBGLN A 315 27.421 −2.664 40.165 1.00 26.90 A ATOM 2400 CG GLN A 31528.328 −3.678 40.846 1.00 29.10 A ATOM 2401 CD GLN A 315 28.375 −5.01240.128 1.00 31.04 A ATOM 2402 OE1 GLN A 315 28.733 −5.083 38.949 1.0032.27 A ATOM 2403 NE2 GLN A 315 28.019 −6.083 40.838 1.00 31.39 A ATOM2404 C GLN A 315 26.787 −0.250 39.928 1.00 25.61 A ATOM 2405 O GLN A 31527.448 0.453 39.166 1.00 25.64 A ATOM 2406 N LYS A 316 25.464 −0.16140.030 1.00 25.14 A ATOM 2407 CA LYS A 316 24.683 0.781 39.232 1.0025.04 A ATOM 2408 CB LYS A 316 23.187 0.591 39.524 1.00 26.09 A ATOM2409 CG LYS A 316 22.251 1.622 38.882 1.00 26.89 A ATOM 2410 CD LYS A316 21.711 1.164 37.528 1.00 27.90 A ATOM 2411 CE LYS A 316 22.772 1.18236.447 1.00 28.93 A ATOM 2412 NZ LYS A 316 22.266 0.658 35.140 1.0027.99 A ATOM 2413 C LYS A 316 25.069 2.238 39.489 1.00 24.49 A ATOM 2414O LYS A 316 25.110 3.046 38.561 1.00 24.40 A ATOM 2415 N LEU A 31725.361 2.571 40.744 1.00 23.79 A ATOM 2416 CA LEU A 317 25.712 3.94141.112 1.00 23.24 A ATOM 2417 CB LEU A 317 24.917 4.344 42.356 1.0023.11 A ATOM 2418 CG LEU A 317 23.407 4.110 42.247 1.00 22.79 A ATOM2419 CD1 LEU A 317 22.780 4.131 43.631 1.00 22.84 A ATOM 2420 CD2 LEU A317 22.786 5.164 41.335 1.00 22.52 A ATOM 2421 C LEU A 317 27.204 4.17541.361 1.00 23.10 A ATOM 2422 O LEU A 317 27.602 5.265 41.773 1.00 23.32A ATOM 2423 N ALA A 318 28.021 3.156 41.115 1.00 22.49 A ATOM 2424 CAALA A 318 29.466 3.253 41.314 1.00 22.25 A ATOM 2425 CB ALA A 318 30.0804.152 40.238 1.00 22.73 A ATOM 2426 C ALA A 318 29.823 3.781 42.705 1.0022.10 A ATOM 2427 O ALA A 318 30.592 4.735 42.837 1.00 21.67 A ATOM 2428N LEU A 319 29.271 3.148 43.738 1.00 21.00 A ATOM 2429 CA LEU A 31929.519 3.546 45.122 1.00 20.63 A ATOM 2430 CB LEU A 319 28.350 3.10446.010 1.00 20.00 A ATOM 2431 CG LEU A 319 26.936 3.586 45.666 1.0019.28 A ATOM 2432 CD1 LEU A 319 25.935 2.999 46.661 1.00 19.38 A ATOM2433 CD2 LEU A 319 26.888 5.099 45.699 1.00 18.96 A ATOM 2434 C LEU A319 30.808 2.944 45.688 1.00 21.45 A ATOM 2435 O LEU A 319 31.163 1.81445.366 1.00 20.80 A ATOM 2436 N LYS A 320 31.498 3.699 46.541 1.00 21.99A ATOM 2437 CA LYS A 320 32.717 3.203 47.173 1.00 23.22 A ATOM 2438 CBLYS A 320 33.413 4.315 47.966 1.00 24.04 A ATOM 2439 CG LYS A 320 33.6955.585 47.170 1.00 26.42 A ATOM 2440 CD LYS A 320 34.439 6.616 48.0141.00 27.32 A ATOM 2441 CE LYS A 320 34.260 8.023 47.455 1.00 28.64 AATOM 2442 NZ LYS A 320 34.606 8.111 46.002 1.00 29.29 A ATOM 2443 C LYSA 320 32.283 2.086 48.128 1.00 23.17 A ATOM 2444 O LYS A 320 31.1622.097 48.634 1.00 23.14 A ATOM 2445 N PRO A 321 33.167 1.114 48.392 1.0023.18 A ATOM 2446 CD PRO A 321 34.535 0.975 47.858 1.00 23.17 A ATOM2447 CA PRO A 321 32.842 −0.001 49.291 1.00 23.00 A ATOM 2448 CB PRO A321 34.174 −0.738 49.416 1.00 23.25 A ATOM 2449 CG PRO A 321 34.812−0.495 48.077 1.00 23.67 A ATOM 2450 C PRO A 321 32.280 0.405 50.6551.00 22.40 A ATOM 2451 O PRO A 321 31.373 −0.239 51.182 1.00 21.92 AATOM 2452 N GLU A 322 32.813 1.482 51.214 1.00 22.04 A ATOM 2453 CA GLUA 322 32.391 1.954 52.528 1.00 21.71 A ATOM 2454 CB GLU A 322 33.3163.088 52.988 1.00 23.36 A ATOM 2455 CG GLU A 322 34.795 2.845 52.7201.00 26.98 A ATOM 2456 CD GLU A 322 35.132 2.879 51.241 1.00 28.13 AATOM 2457 OE1 GLU A 322 34.883 3.918 50.596 1.00 30.06 A ATOM 2458 OE2GLU A 322 35.640 1.867 50.720 1.00 30.37 A ATOM 2459 C GLU A 322 30.9342.429 52.631 1.00 20.23 A ATOM 2460 O GLU A 322 30.368 2.439 53.720 1.0019.87 A ATOM 2461 N LYS A 323 30.326 2.821 51.515 1.00 19.09 A ATOM 2462CA LYS A 323 28.946 3.314 51.555 1.00 18.24 A ATOM 2463 CB LYS A 32328.468 3.697 50.148 1.00 17.68 A ATOM 2464 CG LYS A 323 29.359 4.71949.423 1.00 17.88 A ATOM 2465 CD LYS A 323 29.670 5.951 50.275 1.0018.08 A ATOM 2466 CE LYS A 323 28.407 6.688 50.708 1.00 17.75 A ATOM2467 NZ LYS A 323 28.711 7.892 51.538 1.00 18.08 A ATOM 2468 C LYS A 32327.949 2.330 52.186 1.00 18.18 A ATOM 2469 O LYS A 323 27.091 2.72752.980 1.00 17.44 A ATOM 2470 N MET A 324 28.072 1.050 51.843 1.00 17.79A ATOM 2471 CA MET A 324 27.168 0.022 52.362 1.00 17.73 A ATOM 2472 CBMET A 324 26.926 −1.049 51.290 1.00 17.86 A ATOM 2473 CG MET A 32426.067 −0.601 50.116 1.00 18.32 A ATOM 2474 SD MET A 324 24.323 −0.40550.580 1.00 19.61 A ATOM 2475 CE MET A 324 23.587 0.034 48.988 1.0018.17 A ATOM 2476 C MET A 324 27.619 −0.658 53.657 1.00 17.26 A ATOM2477 O MET A 324 27.054 −1.685 54.044 1.00 17.39 A ATOM 2478 N ASN A 32528.620 −0.099 54.332 1.00 17.04 A ATOM 2479 CA ASN A 325 29.105 −0.68955.578 1.00 16.26 A ATOM 2480 CB ASN A 325 30.138 0.227 56.249 1.0016.89 A ATOM 2481 CG ASN A 325 31.544 0.043 55.694 1.00 17.31 A ATOM2482 OD1 ASN A 325 31.792 −0.825 54.856 1.00 17.48 A ATOM 2483 ND2 ASN A325 32.475 0.865 56.170 1.00 16.86 A ATOM 2484 C ASN A 325 27.996 −1.00056.592 1.00 15.84 A ATOM 2485 O ASN A 325 27.873 −2.134 57.061 1.0015.57 A ATOM 2486 N ALA A 326 27.194 0.006 56.931 1.00 14.81 A ATOM 2487CA ALA A 326 26.127 −0.162 57.918 1.00 14.14 A ATOM 2488 CB ALA A 32625.499 1.199 58.243 1.00 14.41 A ATOM 2489 C ALA A 326 25.043 −1.15257.501 1.00 14.35 A ATOM 2490 O ALA A 326 24.589 −1.967 58.313 1.0014.78 A ATOM 2491 N THR A 327 24.635 −1.079 56.241 1.00 13.41 A ATOM2492 CA THR A 327 23.605 −1.962 55.713 1.00 13.87 A ATOM 2493 CB THR A327 23.242 −1.569 54.259 1.00 13.38 A ATOM 2494 OG1 THR A 327 22.655−0.256 54.253 1.00 13.83 A ATOM 2495 CG2 THR A 327 22.253 −2.570 53.6571.00 13.68 A ATOM 2496 C THR A 327 24.072 −3.421 55.753 1.00 14.01 AATOM 2497 O THR A 327 23.371 −4.288 56.279 1.00 13.75 A ATOM 2498 N ARGA 328 25.259 −3.682 55.211 1.00 14.33 A ATOM 2499 CA ARG A 328 25.814−5.040 55.182 1.00 14.77 A ATOM 2500 CB ARG A 328 27.082 −5.080 54.3161.00 15.22 A ATOM 2501 CG ARG A 328 26.835 −4.886 52.812 1.00 16.37 AATOM 2502 CD ARG A 328 28.148 −4.913 52.021 1.00 18.14 A ATOM 2503 NEARG A 328 27.969 −4.631 50.597 1.00 19.53 A ATOM 2504 CZ ARG A 32827.457 −5.483 49.715 1.00 20.66 A ATOM 2505 NH1 ARG A 328 27.064 −6.68950.102 1.00 22.08 A ATOM 2506 NH2 ARG A 328 27.345 −5.136 48.439 1.0021.33 A ATOM 2507 C ARG A 328 26.116 −5.620 56.573 1.00 15.06 A ATOM2508 O ARG A 328 26.114 −6.836 56.748 1.00 15.82 A ATOM 2509 N GLU A 32926.381 −4.762 57.555 1.00 14.77 A ATOM 2510 CA GLU A 329 26.651 −5.22958.918 1.00 14.81 A ATOM 2511 CB GLU A 329 27.125 −4.067 59.799 1.0015.33 A ATOM 2512 CG GLU A 329 27.244 −4.379 61.293 1.00 17.33 A ATOM2513 CD GLU A 329 28.431 −5.268 61.645 1.00 18.89 A ATOM 2514 OE1 GLU A329 29.282 −5.523 60.764 1.00 18.54 A ATOM 2515 OE2 GLU A 329 28.519−5.702 62.818 1.00 20.32 A ATOM 2516 C GLU A 329 25.378 −5.840 59.5091.00 14.36 A ATOM 2517 O GLU A 329 25.425 −6.885 60.163 1.00 13.91 AATOM 2518 N VAL A 330 24.243 −5.185 59.278 1.00 13.59 A ATOM 2519 CA VALA 330 22.965 −5.676 59.785 1.00 14.02 A ATOM 2520 CB VAL A 330 21.856−4.604 59.629 1.00 13.99 A ATOM 2521 CG1 VAL A 330 20.484 −5.196 59.9681.00 13.58 A ATOM 2522 CG2 VAL A 330 22.157 −3.425 60.556 1.00 14.00 AATOM 2523 C VAL A 330 22.549 −6.968 59.077 1.00 14.02 A ATOM 2524 O VALA 330 22.062 −7.899 59.721 1.00 13.94 A ATOM 2525 N LEU A 331 22.738−7.029 57.759 1.00 13.64 A ATOM 2526 CA LEU A 331 22.399 −8.237 57.0051.00 13.71 A ATOM 2527 CB LEU A 331 22.655 −8.037 55.502 1.00 14.19 AATOM 2528 CG LEU A 331 22.547 −9.303 54.637 1.00 13.98 A ATOM 2529 CD1LEU A 331 21.135 −9.876 54.726 1.00 13.96 A ATOM 2530 CD2 LEU A 33122.894 −8.988 53.189 1.00 14.69 A ATOM 2531 C LEU A 331 23.262 −9.39757.501 1.00 14.26 A ATOM 2532 O LEU A 331 22.792 −10.527 57.647 1.0013.37 A ATOM 2533 N SER A 332 24.531 −9.099 57.760 1.00 15.11 A ATOM2534 CA SER A 332 25.485 −10.097 58.225 1.00 16.35 A ATOM 2535 CB SER A332 26.903 −9.509 58.174 1.00 17.12 A ATOM 2536 OG SER A 332 27.870−10.444 58.619 1.00 19.44 A ATOM 2537 C SER A 332 25.180 −10.602 59.6381.00 16.20 A ATOM 2538 O SER A 332 25.254 −11.799 59.902 1.00 16.47 AATOM 2539 N GLU A 333 24.821 −9.689 60.536 1.00 15.96 A ATOM 2540 CA GLUA 333 24.537 −10.040 61.929 1.00 15.99 A ATOM 2541 CB GLU A 333 24.922−8.872 62.848 1.00 17.32 A ATOM 2542 CG GLU A 333 26.411 −8.541 62.8971.00 20.64 A ATOM 2543 CD GLU A 333 27.242 −9.659 63.496 1.00 22.34 AATOM 2544 OE1 GLU A 333 26.931 −10.096 64.625 1.00 23.49 A ATOM 2545 OE2GLU A 333 28.211 −10.096 62.843 1.00 23.53 A ATOM 2546 C GLU A 33323.105 −10.454 62.279 1.00 14.90 A ATOM 2547 O GLU A 333 22.887 −11.06263.328 1.00 14.01 A ATOM 2548 N TYR A 334 22.135 −10.144 61.421 1.0013.81 A ATOM 2549 CA TYR A 334 20.735 −10.455 61.740 1.00 13.26 A ATOM2550 CB TYR A 334 20.031 −9.174 62.216 1.00 13.56 A ATOM 2551 CG TYR A334 20.683 −8.494 63.398 1.00 14.44 A ATOM 2552 CD1 TYR A 334 20.558−9.018 64.686 1.00 15.41 A ATOM 2553 CE1 TYR A 334 21.191 −8.413 65.7741.00 16.14 A ATOM 2554 CD2 TYR A 334 21.455 −7.342 63.225 1.00 14.72 AATOM 2555 CE2 TYR A 334 22.088 −6.729 64.303 1.00 15.69 A ATOM 2556 CZTYR A 334 21.954 −7.270 65.572 1.00 16.75 A ATOM 2557 OH TYR A 33422.584 −6.668 66.639 1.00 17.76 A ATOM 2558 C TYR A 334 19.878 −11.07160.631 1.00 12.57 A ATOM 2559 O TYR A 334 18.802 −11.600 60.907 1.0012.41 A ATOM 2560 N GLY A 335 20.333 −10.993 59.387 1.00 12.22 A ATOM2561 CA GLY A 335 19.537 −11.522 58.287 1.00 11.80 A ATOM 2562 C GLY A335 18.447 −10.524 57.912 1.00 11.96 A ATOM 2563 O GLY A 335 18.430−9.404 58.429 1.00 11.44 A ATOM 2564 N ASN A 336 17.535 −10.928 57.0281.00 11.66 A ATOM 2565 CA ASN A 336 16.433 −10.071 56.577 1.00 11.70 AATOM 2566 CB ASN A 336 15.957 −10.540 55.189 1.00 11.42 A ATOM 2567 CGASN A 336 14.806 −9.710 54.638 1.00 12.51 A ATOM 2568 OD1 ASN A 33614.090 −9.039 55.382 1.00 13.12 A ATOM 2569 ND2 ASN A 336 14.610 −9.77053.318 1.00 12.55 A ATOM 2570 C ASN A 336 15.272 −10.144 57.573 1.0011.85 A ATOM 2571 O ASN A 336 14.529 −11.132 57.589 1.00 11.61 A ATOM2572 N MET A 337 15.125 −9.103 58.396 1.00 11.75 A ATOM 2573 CA MET A337 14.066 −9.023 59.406 1.00 11.30 A ATOM 2574 CB MET A 337 14.616−8.402 60.702 1.00 11.74 A ATOM 2575 CG MET A 337 15.776 −9.162 61.3471.00 11.23 A ATOM 2576 SD MET A 337 16.500 −8.267 62.775 1.00 12.05 AATOM 2577 CE MET A 337 17.454 −7.023 61.918 1.00 10.68 A ATOM 2578 C META 337 12.872 −8.185 58.912 1.00 11.73 A ATOM 2579 O MET A 337 12.185−7.521 59.705 1.00 11.01 A ATOM 2580 N SER A 338 12.636 −8.220 57.6061.00 10.58 A ATOM 2581 CA SER A 338 11.540 −7.480 56.987 1.00 11.13 AATOM 2582 CB SER A 338 10.194 −8.129 57.344 1.00 11.47 A ATOM 2583 OGSER A 338 9.133 −7.611 56.541 1.00 11.75 A ATOM 2584 C SER A 338 11.539−5.995 57.365 1.00 10.94 A ATOM 2585 O SER A 338 12.580 −5.341 57.3181.00 10.10 A ATOM 2586 N SER A 339 10.380 −5.466 57.753 1.00 10.98 AATOM 2587 CA SER A 339 10.266 −4.044 58.084 1.00 10.99 A ATOM 2588 CBSER A 339 8.838 −3.709 58.543 1.00 11.08 A ATOM 2589 OG SER A 339 8.561−4.237 59.829 1.00 10.91 A ATOM 2590 C SER A 339 11.259 −3.494 59.1071.00 10.72 A ATOM 2591 O SER A 339 11.591 −2.311 59.059 1.00 10.36 AATOM 2592 N ALA A 340 11.743 −4.338 60.015 1.00 10.25 A ATOM 2593 CA ALAA 340 12.678 −3.877 61.048 1.00 10.47 A ATOM 2594 CB ALA A 340 12.734−4.900 62.192 1.00 10.31 A ATOM 2595 C ALA A 340 14.102 −3.553 60.5841.00 10.95 A ATOM 2596 O ALA A 340 14.793 −2.763 61.230 1.00 10.69 AATOM 2597 N CYS A 341 14.542 −4.153 59.480 1.00 11.51 A ATOM 2598 CA CYSA 341 15.907 −3.939 58.978 1.00 12.12 A ATOM 2599 CB CYS A 341 16.080−4.551 57.582 1.00 13.41 A ATOM 2600 SG CYS A 341 16.004 −6.345 57.4971.00 15.80 A ATOM 2601 C CYS A 341 16.407 −2.501 58.911 1.00 11.76 AATOM 2602 O CYS A 341 17.434 −2.167 59.511 1.00 11.11 A ATOM 2603 N VALA 342 15.704 −1.653 58.165 1.00 11.06 A ATOM 2604 CA VAL A 342 16.152−0.274 58.010 1.00 11.17 A ATOM 2605 CB VAL A 342 15.254 0.506 57.0211.00 10.53 A ATOM 2606 CG1 VAL A 342 15.371 −0.118 55.637 1.00 10.75 AATOM 2607 CG2 VAL A 342 13.812 0.501 57.493 1.00 10.96 A ATOM 2608 C VALA 342 16.266 0.487 59.321 1.00 10.94 A ATOM 2609 O VAL A 342 17.0481.436 59.423 1.00 11.24 A ATOM 2610 N LEU A 343 15.501 0.073 60.328 1.0010.28 A ATOM 2611 CA LEU A 343 15.576 0.736 61.623 1.00 9.58 A ATOM 2612CB LEU A 343 14.298 0.479 62.435 1.00 9.47 A ATOM 2613 CG LEU A 34313.005 0.940 61.735 1.00 9.16 A ATOM 2614 CD1 LEU A 343 11.828 0.84162.708 1.00 9.75 A ATOM 2615 CD2 LEU A 343 13.160 2.381 61.236 1.0010.29 A ATOM 2616 C LEU A 343 16.832 0.261 62.374 1.00 9.66 A ATOM 2617O LEU A 343 17.470 1.051 63.073 1.00 9.55 A ATOM 2618 N PHE A 344 17.197−1.014 62.223 1.00 10.11 A ATOM 2619 CA PHE A 344 18.417 −1.525 62.8581.00 10.35 A ATOM 2620 CB PHE A 344 18.593 −3.040 62.626 1.00 10.60 AATOM 2621 CG PHE A 344 17.946 −3.924 63.674 1.00 11.60 A ATOM 2622 CD1PHE A 344 16.560 −4.063 63.743 1.00 11.33 A ATOM 2623 CD2 PHE A 34418.737 −4.673 64.551 1.00 12.06 A ATOM 2624 CE1 PHE A 344 15.970 −4.93964.664 1.00 12.07 A ATOM 2625 CE2 PHE A 344 18.162 −5.551 65.477 1.0012.12 A ATOM 2626 CZ PHE A 344 16.773 −5.686 65.533 1.00 12.33 A ATOM2627 C PHE A 344 19.605 −0.804 62.204 1.00 10.33 A ATOM 2628 O PHE A 34420.588 −0.460 62.870 1.00 9.78 A ATOM 2629 N ILE A 345 19.514 −0.57460.895 1.00 9.91 A ATOM 2630 CA ILE A 345 20.598 0.092 60.168 1.00 10.19A ATOM 2631 CB ILE A 345 20.360 0.029 58.632 1.00 9.96 A ATOM 2632 CG2ILE A 345 21.463 0.791 57.893 1.00 9.91 A ATOM 2633 CG1 ILE A 345 20.345−1.438 58.180 1.00 10.15 A ATOM 2634 CD1 ILE A 345 19.967 −1.653 56.7221.00 9.55 A ATOM 2635 C ILE A 345 20.798 1.539 60.624 1.00 10.60 A ATOM2636 O ILE A 345 21.938 2.006 60.728 1.00 11.29 A ATOM 2637 N LEU A 34619.706 2.254 60.889 1.00 10.89 A ATOM 2638 CA LEU A 346 19.809 3.63361.375 1.00 11.20 A ATOM 2639 CB LEU A 346 18.414 4.251 61.580 1.0010.69 A ATOM 2640 CG LEU A 346 17.624 4.627 60.321 1.00 10.61 A ATOM2641 CD1 LEU A 346 16.187 4.996 60.695 1.00 11.25 A ATOM 2642 CD2 LEU A346 18.313 5.790 59.617 1.00 11.23 A ATOM 2643 C LEU A 346 20.561 3.62762.707 1.00 11.84 A ATOM 2644 O LEU A 346 21.406 4.492 62.965 1.00 12.64A ATOM 2645 N ASP A 347 20.258 2.644 63.550 1.00 12.06 A ATOM 2646 CAASP A 347 20.908 2.537 64.857 1.00 13.39 A ATOM 2647 CB ASP A 347 20.2171.450 65.690 1.00 13.78 A ATOM 2648 CG ASP A 347 20.591 1.508 67.1631.00 15.67 A ATOM 2649 OD1 ASP A 347 20.710 2.629 67.706 1.00 14.75 AATOM 2650 OD2 ASP A 347 20.746 0.432 67.783 1.00 15.69 A ATOM 2651 C ASPA 347 22.408 2.245 64.710 1.00 13.67 A ATOM 2652 O ASP A 347 23.2392.873 65.367 1.00 13.64 A ATOM 2653 N GLU A 348 22.751 1.301 63.838 1.0014.56 A ATOM 2654 CA GLU A 348 24.147 0.938 63.592 1.00 15.36 A ATOM2655 CB GLU A 348 24.215 −0.210 62.579 1.00 16.27 A ATOM 2656 CG GLU A348 25.617 −0.592 62.092 1.00 17.76 A ATOM 2657 CD GLU A 348 26.541−1.082 63.200 1.00 18.78 A ATOM 2658 OE1 GLU A 348 26.047 −1.562 64.2421.00 19.58 A ATOM 2659 OE2 GLU A 348 27.773 −1.002 63.019 1.00 19.89 AATOM 2660 C GLU A 348 24.946 2.134 63.071 1.00 15.06 A ATOM 2661 O GLU A348 26.049 2.405 63.541 1.00 14.81 A ATOM 2662 N MET A 349 24.388 2.85362.104 1.00 14.78 A ATOM 2663 CA MET A 349 25.079 4.008 61.540 1.0015.19 A ATOM 2664 CB MET A 349 24.265 4.625 60.401 1.00 15.22 A ATOM2665 CG MET A 349 24.931 5.857 59.811 1.00 17.23 A ATOM 2666 SD MET A349 24.032 6.538 58.421 1.00 18.52 A ATOM 2667 CE MET A 349 24.320 5.23857.186 1.00 16.39 A ATOM 2668 C MET A 349 25.390 5.100 62.563 1.00 14.73A ATOM 2669 O MET A 349 26.503 5.624 62.599 1.00 14.30 A ATOM 2670 N ARGA 350 24.409 5.453 63.384 1.00 14.34 A ATOM 2671 CA ARG A 350 24.6156.498 64.379 1.00 15.08 A ATOM 2672 CB ARG A 350 23.272 6.950 64.9621.00 14.45 A ATOM 2673 CG ARG A 350 22.518 5.897 65.756 1.00 14.44 AATOM 2674 CD ARG A 350 22.510 6.236 67.247 1.00 14.54 A ATOM 2675 NE ARGA 350 21.567 5.396 67.984 1.00 14.41 A ATOM 2676 CZ ARG A 350 21.0135.735 69.144 1.00 14.88 A ATOM 2677 NH1 ARG A 350 21.308 6.902 69.7011.00 14.87 A ATOM 2678 NH2 ARG A 350 20.159 4.912 69.745 1.00 14.52 AATOM 2679 C ARG A 350 25.571 6.066 65.492 1.00 15.83 A ATOM 2680 O ARG A350 26.360 6.873 65.987 1.00 15.01 A ATOM 2681 N LYS A 351 25.514 4.79565.880 1.00 16.14 A ATOM 2682 CA LYS A 351 26.411 4.305 66.921 1.0017.27 A ATOM 2683 CB LYS A 351 25.988 2.909 67.382 1.00 18.64 A ATOM2684 CG LYS A 351 24.844 2.916 68.386 1.00 20.60 A ATOM 2685 CD LYS A351 24.438 1.494 68.767 1.00 22.37 A ATOM 2686 CE LYS A 351 23.636 1.48070.061 1.00 23.69 A ATOM 2687 NZ LYS A 351 22.393 2.293 69.986 1.0024.80 A ATOM 2688 C LYS A 351 27.860 4.286 66.430 1.00 17.14 A ATOM 2689O LYS A 351 28.771 4.696 67.152 1.00 16.83 A ATOM 2690 N LYS A 35228.073 3.817 65.203 1.00 16.98 A ATOM 2691 CA LYS A 352 29.419 3.76764.627 1.00 17.64 A ATOM 2692 CB LYS A 352 29.416 2.966 63.323 1.0018.76 A ATOM 2693 CG LYS A 352 29.490 1.470 63.526 1.00 21.91 A ATOM2694 CD LYS A 352 30.857 1.068 64.077 1.00 23.41 A ATOM 2695 CE LYS A352 30.896 −0.405 64.432 1.00 24.84 A ATOM 2696 NZ LYS A 352 29.886−0.731 65.483 1.00 26.79 A ATOM 2697 C LYS A 352 29.995 5.156 64.3631.00 17.19 A ATOM 2698 O LYS A 352 31.204 5.369 64.500 1.00 16.04 A ATOM2699 N SER A 353 29.138 6.094 63.970 1.00 16.74 A ATOM 2700 CA SER A 35329.583 7.460 63.710 1.00 17.39 A ATOM 2701 CB SER A 353 28.435 8.29763.138 1.00 17.32 A ATOM 2702 OG SER A 353 28.067 7.843 61.848 1.0016.97 A ATOM 2703 C SER A 353 30.073 8.088 65.012 1.00 18.27 A ATOM 2704O SER A 353 31.043 8.850 65.025 1.00 18.81 A ATOM 2705 N THR A 35429.391 7.768 66.106 1.00 18.39 A ATOM 2706 CA THR A 354 29.749 8.29067.420 1.00 19.76 A ATOM 2707 CB THR A 354 28.618 8.011 68.435 1.0020.00 A ATOM 2708 OG1 THR A 354 27.443 8.729 68.043 1.00 20.37 A ATOM2709 CG2 THR A 354 29.027 8.435 69.839 1.00 20.74 A ATOM 2710 C THR A354 31.036 7.618 67.899 1.00 20.00 A ATOM 2711 O THR A 354 31.959 8.27268.399 1.00 19.48 A ATOM 2712 N GLN A 355 31.080 6.303 67.730 1.00 20.15A ATOM 2713 CA GLN A 355 32.222 5.493 68.128 1.00 21.65 A ATOM 2714 CBGLN A 355 31.913 4.019 67.837 1.00 22.91 A ATOM 2715 CG GLN A 355 33.0953.066 67.958 1.00 25.78 A ATOM 2716 CD GLN A 355 32.778 1.685 67.4051.00 27.34 A ATOM 2717 OE1 GLN A 355 31.862 1.009 67.874 1.00 29.12 AATOM 2718 NE2 GLN A 355 33.532 1.264 66.398 1.00 28.38 A ATOM 2719 C GLNA 355 33.530 5.889 67.432 1.00 21.31 A ATOM 2720 O GLN A 355 34.5626.071 68.086 1.00 21.87 A ATOM 2721 N ASN A 356 33.488 6.027 66.111 1.0020.41 A ATOM 2722 CA ASN A 356 34.692 6.352 65.356 1.00 20.53 A ATOM2723 CB ASN A 356 34.655 5.657 63.992 1.00 21.37 A ATOM 2724 CG ASN A356 34.710 4.143 64.116 1.00 22.05 A ATOM 2725 OD1 ASN A 356 35.3403.608 65.029 1.00 22.39 A ATOM 2726 ND2 ASN A 356 34.060 3.447 63.1931.00 23.15 A ATOM 2727 C ASN A 356 35.027 7.829 65.182 1.00 19.88 A ATOM2728 O ASN A 356 35.927 8.179 64.413 1.00 19.58 A ATOM 2729 N GLY A 35734.301 8.687 65.894 1.00 19.15 A ATOM 2730 CA GLY A 357 34.563 10.11765.848 1.00 18.39 A ATOM 2731 C GLY A 357 34.155 10.930 64.634 1.0018.00 A ATOM 2732 O GLY A 357 34.839 11.896 64.289 1.00 17.19 A ATOM2733 N LEU A 358 33.056 10.564 63.982 1.00 17.83 A ATOM 2734 CA LEU A358 32.599 11.325 62.819 1.00 18.37 A ATOM 2735 CB LEU A 358 31.64110.487 61.960 1.00 18.29 A ATOM 2736 CG LEU A 358 32.261 9.431 61.0331.00 18.70 A ATOM 2737 CD1 LEU A 358 33.183 10.113 60.032 1.00 18.64 AATOM 2738 CD2 LEU A 358 33.028 8.392 61.841 1.00 18.14 A ATOM 2739 C LEUA 358 31.905 12.589 63.329 1.00 18.28 A ATOM 2740 O LEU A 358 31.43012.621 64.465 1.00 19.60 A ATOM 2741 N LYS A 359 31.847 13.625 62.4971.00 18.13 A ATOM 2742 CA LYS A 359 31.245 14.894 62.902 1.00 18.17 AATOM 2743 CB LYS A 359 31.862 16.033 62.085 1.00 19.78 A ATOM 2744 CGLYS A 359 33.378 16.146 62.242 1.00 22.00 A ATOM 2745 CD LYS A 35933.773 16.502 63.672 1.00 24.21 A ATOM 2746 CE LYS A 359 33.331 17.91564.027 1.00 26.14 A ATOM 2747 NZ LYS A 359 33.637 18.270 65.443 1.0027.55 A ATOM 2748 C LYS A 359 29.713 14.990 62.861 1.00 17.59 A ATOM2749 O LYS A 359 29.147 15.972 63.337 1.00 17.60 A ATOM 2750 N THR A 36029.046 13.992 62.286 1.00 16.40 A ATOM 2751 CA THR A 360 27.577 13.97562.247 1.00 15.45 A ATOM 2752 CB THR A 360 26.992 14.499 60.911 1.0015.82 A ATOM 2753 OG1 THR A 360 27.231 13.539 59.877 1.00 15.65 A ATOM2754 CG2 THR A 360 27.613 15.840 60.524 1.00 16.52 A ATOM 2755 C THR A360 27.116 12.532 62.413 1.00 14.68 A ATOM 2756 O THR A 360 27.89711.598 62.215 1.00 14.27 A ATOM 2757 N THR A 361 25.852 12.348 62.7771.00 13.61 A ATOM 2758 CA THR A 361 25.307 11.008 62.965 1.00 13.33 AATOM 2759 CB THR A 361 23.919 11.066 63.629 1.00 13.09 A ATOM 2760 OG1THR A 361 23.093 11.988 62.915 1.00 12.47 A ATOM 2761 CG2 THR A 36124.043 11.529 65.081 1.00 13.05 A ATOM 2762 C THR A 361 25.194 10.25661.645 1.00 13.18 A ATOM 2763 O THR A 361 24.936 9.050 61.633 1.00 13.52A ATOM 2764 N GLY A 362 25.394 10.973 60.542 1.00 13.05 A ATOM 2765 CAGLY A 362 25.325 10.368 59.222 1.00 13.54 A ATOM 2766 C GLY A 362 26.69310.220 58.572 1.00 13.80 A ATOM 2767 O GLY A 362 26.921 10.676 57.4471.00 13.72 A ATOM 2768 N GLU A 363 27.606 9.578 59.292 1.00 14.30 A ATOM2769 CA GLU A 363 28.969 9.342 58.823 1.00 14.87 A ATOM 2770 CB GLU A363 28.951 8.326 57.672 1.00 15.38 A ATOM 2771 CG GLU A 363 28.092 7.10158.010 1.00 16.94 A ATOM 2772 CD GLU A 363 28.216 5.954 57.023 1.0017.95 A ATOM 2773 OE1 GLU A 363 28.357 6.202 55.808 1.00 18.60 A ATOM2774 OE2 GLU A 363 28.144 4.789 57.472 1.00 19.19 A ATOM 2775 C GLU A363 29.682 10.634 58.414 1.00 15.17 A ATOM 2776 O GLU A 363 30.48110.655 57.475 1.00 14.88 A ATOM 2777 N GLY A 364 29.388 11.711 59.1361.00 15.36 A ATOM 2778 CA GLY A 364 30.023 12.986 58.851 1.00 16.19 AATOM 2779 C GLY A 364 29.429 13.764 57.693 1.00 16.44 A ATOM 2780 O GLYA 364 29.856 14.884 57.418 1.00 16.69 A ATOM 2781 N LEU A 365 28.44513.184 57.012 1.00 16.46 A ATOM 2782 CA LEU A 365 27.813 13.853 55.8801.00 16.91 A ATOM 2783 CB LEU A 365 27.494 12.831 54.786 1.00 16.94 AATOM 2784 CG LEU A 365 28.696 11.997 54.320 1.00 17.07 A ATOM 2785 CD1LEU A 365 28.228 10.876 53.405 1.00 17.97 A ATOM 2786 CD2 LEU A 36529.703 12.889 53.610 1.00 16.75 A ATOM 2787 C LEU A 365 26.544 14.58756.323 1.00 16.99 A ATOM 2788 O LEU A 365 26.039 14.354 57.421 1.0017.16 A ATOM 2789 N GLU A 366 26.034 15.469 55.467 1.00 16.87 A ATOM2790 CA GLU A 366 24.838 16.252 55.787 1.00 17.25 A ATOM 2791 CB GLU A366 24.941 17.644 55.144 1.00 19.11 A ATOM 2792 CG GLU A 366 23.62918.432 55.109 1.00 21.19 A ATOM 2793 CD GLU A 366 23.828 19.896 54.7581.00 22.96 A ATOM 2794 OE1 GLU A 366 24.687 20.198 53.905 1.00 23.65 AATOM 2795 OE2 GLU A 366 23.111 20.748 55.328 1.00 24.80 A ATOM 2796 CGLU A 366 23.499 15.611 55.410 1.00 16.91 A ATOM 2797 O GLU A 366 22.58915.540 56.244 1.00 16.56 A ATOM 2798 N TRP A 367 23.374 15.153 54.1681.00 15.76 A ATOM 2799 CA TRP A 367 22.127 14.535 53.703 1.00 15.43 AATOM 2800 CB TRP A 367 21.699 15.136 52.358 1.00 15.92 A ATOM 2801 CGTRP A 367 21.584 16.640 52.362 1.00 17.29 A ATOM 2802 CD2 TRP A 36720.521 17.420 52.924 1.00 17.28 A ATOM 2803 CE2 TRP A 367 20.843 18.78152.714 1.00 17.73 A ATOM 2804 CE3 TRP A 367 19.327 17.101 53.587 1.0017.91 A ATOM 2805 CD1 TRP A 367 22.483 17.535 51.848 1.00 17.11 A ATOM2806 NE1 TRP A 367 22.043 18.823 52.054 1.00 17.26 A ATOM 2807 CZ2 TRP A367 20.014 19.823 53.142 1.00 18.10 A ATOM 2808 CZ3 TRP A 367 18.50018.139 54.014 1.00 17.80 A ATOM 2809 CH2 TRP A 367 18.849 19.483 53.7891.00 18.48 A ATOM 2810 C TRP A 367 22.243 13.021 53.551 1.00 14.85 AATOM 2811 O TRP A 367 23.335 12.493 53.340 1.00 14.03 A ATOM 2812 N GLYA 368 21.105 12.333 53.643 1.00 13.90 A ATOM 2813 CA GLY A 368 21.09310.883 53.510 1.00 13.64 A ATOM 2814 C GLY A 368 19.786 10.357 52.9391.00 12.46 A ATOM 2815 O GLY A 368 18.826 11.110 52.773 1.00 13.28 AATOM 2816 N VAL A 369 19.739 9.064 52.633 1.00 12.00 A ATOM 2817 CA VALA 369 18.530 8.470 52.077 1.00 11.30 A ATOM 2818 CB VAL A 369 18.6348.356 50.533 1.00 11.23 A ATOM 2819 CG1 VAL A 369 19.762 7.405 50.1551.00 10.95 A ATOM 2820 CG2 VAL A 369 17.316 7.871 49.952 1.00 11.34 AATOM 2821 C VAL A 369 18.265 7.083 52.656 1.00 11.73 A ATOM 2822 O VAL A369 19.198 6.334 52.936 1.00 11.94 A ATOM 2823 N LEU A 370 16.989 6.75952.848 1.00 11.77 A ATOM 2824 CA LEU A 370 16.580 5.456 53.371 1.0011.76 A ATOM 2825 CB LEU A 370 15.911 5.606 54.749 1.00 11.28 A ATOM2826 CG LEU A 370 15.397 4.333 55.445 1.00 11.66 A ATOM 2827 CD1 LEU A370 15.368 4.547 56.960 1.00 11.65 A ATOM 2828 CD2 LEU A 370 14.0153.962 54.918 1.00 12.29 A ATOM 2829 C LEU A 370 15.595 4.857 52.376 1.0011.86 A ATOM 2830 O LEU A 370 14.646 5.527 51.971 1.00 11.90 A ATOM 2831N PHE A 371 15.828 3.604 51.984 1.00 11.79 A ATOM 2832 CA PHE A 37114.968 2.912 51.027 1.00 11.80 A ATOM 2833 CB PHE A 371 15.755 2.52849.761 1.00 12.26 A ATOM 2834 CG PHE A 371 16.049 3.680 48.835 1.0013.18 A ATOM 2835 CD1 PHE A 371 15.017 4.364 48.199 1.00 13.53 A ATOM2836 CD2 PHE A 371 17.364 4.053 48.569 1.00 13.39 A ATOM 2837 CE1 PHE A371 15.291 5.401 47.309 1.00 14.13 A ATOM 2838 CE2 PHE A 371 17.6505.090 47.680 1.00 14.61 A ATOM 2839 CZ PHE A 371 16.612 5.765 47.0491.00 14.39 A ATOM 2840 C PHE A 371 14.350 1.633 51.580 1.00 11.83 A ATOM2841 O PHE A 371 15.024 0.837 52.242 1.00 11.89 A ATOM 2842 N GLY A 37213.069 1.442 51.278 1.00 11.66 A ATOM 2843 CA GLY A 372 12.357 0.23851.677 1.00 11.23 A ATOM 2844 C GLY A 372 11.875 −0.413 50.386 1.0012.03 A ATOM 2845 O GLY A 372 11.381 0.290 49.504 1.00 11.11 A ATOM 2846N PHE A 373 12.034 −1.732 50.254 1.00 12.31 A ATOM 2847 CA PHE A 37311.604 −2.446 49.043 1.00 12.91 A ATOM 2848 CB PHE A 373 12.815 −3.02648.281 1.00 13.68 A ATOM 2849 CG PHE A 373 13.966 −2.063 48.107 1.0014.91 A ATOM 2850 CD1 PHE A 373 13.784 −0.832 47.485 1.00 15.93 A ATOM2851 CD2 PHE A 373 15.245 −2.406 48.547 1.00 15.06 A ATOM 2852 CE1 PHE A373 14.859 0.046 47.303 1.00 16.22 A ATOM 2853 CE2 PHE A 373 16.327−1.538 48.372 1.00 15.66 A ATOM 2854 CZ PHE A 373 16.133 −0.309 47.7491.00 15.82 A ATOM 2855 C PHE A 373 10.698 −3.609 49.450 1.00 12.82 AATOM 2856 O PHE A 373 10.962 −4.269 50.455 1.00 11.69 A ATOM 2857 N GLYA 374 9.650 −3.879 48.672 1.00 13.46 A ATOM 2858 CA GLY A 374 8.756−4.979 49.019 1.00 14.44 A ATOM 2859 C GLY A 374 7.629 −5.288 48.0411.00 15.41 A ATOM 2860 O GLY A 374 7.630 −4.787 46.916 1.00 15.04 A ATOM2861 N PRO A 375 6.639 −6.108 48.457 1.00 16.00 A ATOM 2862 CD PRO A 3756.560 −6.647 49.828 1.00 16.19 A ATOM 2863 CA PRO A 375 5.467 −6.53847.680 1.00 16.73 A ATOM 2864 CB PRO A 375 4.529 −7.081 48.751 1.0016.44 A ATOM 2865 CG PRO A 375 5.475 −7.711 49.703 1.00 16.06 A ATOM2866 C PRO A 375 4.799 −5.474 46.820 1.00 18.46 A ATOM 2867 O PRO A 3754.691 −4.298 47.206 1.00 17.70 A ATOM 2868 N GLY A 376 4.319 −5.91545.660 1.00 20.24 A ATOM 2869 CA GLY A 376 3.682 −5.010 44.731 1.0021.94 A ATOM 2870 C GLY A 376 4.800 −4.070 44.412 1.00 23.04 A ATOM 2871O GLY A 376 4.606 −2.851 44.335 1.00 24.98 A ATOM 2872 N LEU A 377 5.977−4.666 44.214 1.00 22.83 A ATOM 2873 CA LEU A 377 7.203 −3.935 43.9631.00 20.77 A ATOM 2874 CB LEU A 377 7.742 −4.194 42.562 1.00 22.54 AATOM 2875 CG LEU A 377 8.891 −5.198 42.724 1.00 23.55 A ATOM 2876 CD1LEU A 377 9.542 −5.485 41.399 1.00 24.83 A ATOM 2877 CD2 LEU A 377 9.919−4.634 43.709 1.00 23.91 A ATOM 2878 C LEU A 377 7.042 −2.465 44.2401.00 19.02 A ATOM 2879 O LEU A 377 6.897 −1.629 43.344 1.00 17.12 A ATOM2880 N THR A 378 7.057 −2.194 45.537 1.00 16.80 A ATOM 2881 CA THR A 3786.910 −0.873 46.096 1.00 14.86 A ATOM 2882 CB THR A 378 5.954 −0.91847.319 1.00 14.08 A ATOM 2883 OG1 THR A 378 4.660 −1.385 46.905 1.0015.17 A ATOM 2884 CG2 THR A 378 5.825 0.455 47.954 1.00 13.38 A ATOM2885 C THR A 378 8.279 −0.393 46.565 1.00 14.33 A ATOM 2886 O THR A 3789.075 −1.172 47.104 1.00 13.55 A ATOM 2887 N ILE A 379 8.553 0.88546.339 1.00 13.27 A ATOM 2888 CA ILE A 379 9.803 1.500 46.772 1.00 12.71A ATOM 2889 CB ILE A 379 10.649 2.010 45.570 1.00 13.23 A ATOM 2890 CG2ILE A 379 11.892 2.740 46.078 1.00 13.06 A ATOM 2891 CG1 ILE A 37911.066 0.837 44.678 1.00 14.08 A ATOM 2892 CD1 ILE A 379 11.854 1.24743.439 1.00 15.36 A ATOM 2893 C ILE A 379 9.425 2.703 47.633 1.00 12.32A ATOM 2894 O ILE A 379 8.763 3.615 47.151 1.00 12.02 A ATOM 2895 N GLUA 380 9.804 2.682 48.911 1.00 11.67 A ATOM 2896 CA GLU A 380 9.532 3.80349.808 1.00 11.50 A ATOM 2897 CB GLU A 380 9.123 3.317 51.212 1.00 11.02A ATOM 2898 CG GLU A 380 7.764 2.601 51.299 1.00 11.78 A ATOM 2899 CDGLU A 380 6.607 3.522 51.695 1.00 11.77 A ATOM 2900 OE1 GLU A 380 6.8194.747 51.805 1.00 11.99 A ATOM 2901 OE2 GLU A 380 5.479 3.019 51.8971.00 11.77 A ATOM 2902 C GLU A 380 10.848 4.576 49.907 1.00 11.95 A ATOM2903 O GLU A 380 11.912 3.971 50.076 1.00 11.95 A ATOM 2904 N THR A 38110.773 5.900 49.783 1.00 12.03 A ATOM 2905 CA THR A 381 11.951 6.76349.867 1.00 12.38 A ATOM 2906 CB THR A 381 12.186 7.570 48.552 1.0013.41 A ATOM 2907 OG1 THR A 381 12.202 6.690 47.422 1.00 14.31 A ATOM2908 CG2 THR A 381 13.522 8.311 48.613 1.00 13.86 A ATOM 2909 C THR A381 11.777 7.791 50.987 1.00 12.43 A ATOM 2910 O THR A 381 10.747 8.46651.062 1.00 12.02 A ATOM 2911 N VAL A 382 12.778 7.900 51.860 1.00 12.62A ATOM 2912 CA VAL A 382 12.754 8.882 52.942 1.00 13.01 A ATOM 2913 CBVAL A 382 12.626 8.229 54.346 1.00 12.57 A ATOM 2914 CG1 VAL A 38212.612 9.321 55.414 1.00 12.79 A ATOM 2915 CG2 VAL A 382 11.362 7.38054.433 1.00 12.77 A ATOM 2916 C VAL A 382 14.062 9.678 52.933 1.00 13.29A ATOM 2917 O VAL A 382 15.140 9.109 53.128 1.00 13.54 A ATOM 2918 N VALA 383 13.977 10.984 52.692 1.00 13.17 A ATOM 2919 CA VAL A 383 15.17811.819 52.698 1.00 13.33 A ATOM 2920 CB VAL A 383 15.024 13.063 51.7931.00 13.72 A ATOM 2921 CG1 VAL A 383 16.291 13.928 51.870 1.00 13.77 AATOM 2922 CG2 VAL A 383 14.782 12.628 50.356 1.00 14.43 A ATOM 2923 CVAL A 383 15.438 12.264 54.136 1.00 12.88 A ATOM 2924 O VAL A 383 14.52212.687 54.845 1.00 12.31 A ATOM 2925 N LEU A 384 16.694 12.168 54.5591.00 13.47 A ATOM 2926 CA LEU A 384 17.083 12.520 55.922 1.00 13.63 AATOM 2927 CB LEU A 384 17.542 11.257 56.662 1.00 13.93 A ATOM 2928 CGLEU A 384 16.574 10.078 56.767 1.00 12.86 A ATOM 2929 CD1 LEU A 38417.339 8.831 57.206 1.00 12.88 A ATOM 2930 CD2 LEU A 384 15.465 10.40657.752 1.00 12.99 A ATOM 2931 C LEU A 384 18.214 13.543 55.988 1.0014.36 A ATOM 2932 O LEU A 384 18.951 13.734 55.022 1.00 14.08 A ATOM2933 N ARG A 385 18.330 14.199 57.140 1.00 14.44 A ATOM 2934 CA ARG A385 19.402 15.163 57.400 1.00 15.65 A ATOM 2935 CB ARG A 385 18.85816.594 57.540 1.00 16.91 A ATOM 2936 CG ARG A 385 19.954 17.674 57.6301.00 19.02 A ATOM 2937 CD ARG A 385 19.381 19.100 57.574 1.00 20.86 AATOM 2938 NE ARG A 385 20.430 20.114 57.422 1.00 23.18 A ATOM 2939 CZARG A 385 21.158 20.611 58.419 1.00 24.39 A ATOM 2940 NH1 ARG A 38520.960 20.202 59.663 1.00 25.40 A ATOM 2941 NH2 ARG A 385 22.096 21.51858.171 1.00 25.36 A ATOM 2942 C ARG A 385 20.001 14.701 58.731 1.0015.04 A ATOM 2943 O ARG A 385 19.268 14.342 59.653 1.00 14.72 A ATOM2944 N SER A 386 21.326 14.683 58.823 1.00 14.39 A ATOM 2945 CA SER A386 21.992 14.242 60.043 1.00 14.75 A ATOM 2946 CB SER A 386 23.42213.803 59.732 1.00 14.25 A ATOM 2947 OG SER A 386 24.170 14.898 59.2351.00 14.91 A ATOM 2948 C SER A 386 22.030 15.347 61.093 1.00 14.95 AATOM 2949 O SER A 386 21.565 16.465 60.855 1.00 14.63 A ATOM 2950 N VALA 387 22.592 15.014 62.252 1.00 15.31 A ATOM 2951 CA VAL A 387 22.73415.943 63.369 1.00 16.50 A ATOM 2952 CB VAL A 387 21.947 15.452 64.6061.00 16.07 A ATOM 2953 CG1 VAL A 387 22.214 16.364 65.796 1.00 15.48 AATOM 2954 CG2 VAL A 387 20.457 15.408 64.287 1.00 15.50 A ATOM 2955 CVAL A 387 24.218 16.025 63.735 1.00 18.05 A ATOM 2956 O VAL A 387 24.91215.006 63.750 1.00 17.63 A ATOM 2957 N ALA A 388 24.693 17.233 64.0301.00 19.63 A ATOM 2958 CA ALA A 388 26.095 17.455 64.389 1.00 22.13 AATOM 2959 CB ALA A 388 26.325 18.931 64.711 1.00 22.23 A ATOM 2960 C ALAA 388 26.548 16.588 65.560 1.00 23.82 A ATOM 2961 O ALA A 388 25.89016.540 66.601 1.00 24.03 A ATOM 2962 N ILE A 389 27.689 15.926 65.3661.00 25.95 A ATOM 2963 CA ILE A 389 28.306 15.023 66.338 1.00 27.95 AATOM 2964 CB ILE A 389 28.605 15.734 67.679 1.00 28.69 A ATOM 2965 CG2ILE A 389 28.958 14.707 68.752 1.00 29.02 A ATOM 2966 CG1 ILE A 38929.788 16.693 67.512 1.00 28.93 A ATOM 2967 CD1 ILE A 389 29.524 17.87166.590 1.00 29.88 A ATOM 2968 C ILE A 389 27.470 13.775 66.607 1.0028.74 A ATOM 2969 OT1 ILE A 389 27.939 12.668 66.256 1.00 28.79 A ATOM2970 OT2 ILE A 389 26.354 13.915 67.157 1.00 29.65 A

1. A method of producing a mutant chalcone synthase with alteredsubstrate specificity, said method comprising substituting one or moreamino acids of wild type chalcone synthase of SEQ ID NO:1 with the aminoacid residues at the corresponding positions in a model structure of aplant polyketide synthase, wherein said one or more amino acids to besubstituted are selected from the group consisting of positions 96, 98,99, 100, 131, 133, 134, 135, 137, 157, 158, 159, 160, 165, 255, 257,258, 266, 268, 269, 270 and 273 of SEQ ID NO:1, thereby producing saidmutant chalcone synthase having altered substrate specificity.
 2. Themethod of claim 1, wherein said wild type chalcone synthase comprises atleast fourteen active site α-carbons having the structural coordinatesof Table 1 (SEQ ID NO:1).
 3. The method of claim 1, wherein said one ormore substitutions are selected from the group consisting of D96A, V98L,V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V,Y160F, Q165H, D255G, H257K, L258V, H266Q, L268K, K269G, D270A and G273D.4. The method of claim 1, wherein said one or more amino acids comprisesubstitutions at each of positions 98, 131, 133, 134, 135 and
 137. 5.The method of claim 4, wherein the substitutions comprise V98L, T131S,S133T, G134T, V135P, and M137L.
 6. The method of claim 4, wherein saidone or more amino acids further comprise substitutions at each ofpositions 96, 99 and
 100. 7. The method of claim 5, wherein thesubstitutions further comprise D96A, V99A and V100M.
 8. The method ofclaim 4, wherein said one or more amino acids further comprisesubstitutions at each of positions 158 and
 160. 9. The method of claim5, wherein the substitutions further comprise M158G and Y160F.
 10. Themethod of claim 6, wherein said one or more amino acids further comprisesubstitutions at each of positions 158, 160 and
 269. 11. The method ofclaim 7, wherein the substitutions further comprise M158G, Y160F andK269G.
 12. The method of claim 8, wherein said one or more amino acidsfurther comprise substitutions at each of positions 156, 159 and 165.13. The method of claim 9, wherein the substitutions further compriseY157V, M159V and Q165H.
 14. The method of claim 10, wherein said one ormore amino acids further comprise substitutions at each of positions156, 158, 164, 267, 270 and
 273. 15. The method of claim 11, wherein thesubstitutions further comprise Y157V, M159V, Q165H, L268K, D270A andG273D.
 16. The method of claim 14, wherein said one or more amino acidsfurther comprise substitutions at each of positions 254, 256, 258 and266.
 17. The method of claim 15, wherein the substitutions furthercomprise D255G, H257K, L258V and H266Q.
 18. The method of claim 1,wherein said plant polyketide synthase is a stilbene synthase.
 19. Themethod of claim 1, wherein said mutant chalcone synthase is produced invitro.
 20. The method of claim 1, wherein said mutant chalcone synthaseis produced in vivo.
 21. The method of claim 20, wherein said mutantchalcone synthase is produced in a plant.
 22. A method of producing amutant chalcone synthase with altered substrate specificity, said methodcomprising: expressing an enzymatically active mutant chalcone synthasegenerated by substituting one or more amino acids of wild type chalconesynthase of SEQ ID NO:1 with one or more amino acid residues at thecorresponding positions of a plant polyketide synthase, wherein said oneor more amino acids to be substituted are selected from the groupconsisting of positions 96, 98, 99, 100, 131, 133, 134, 135, 137, 157,158, 159, 160, 165, 255, 257, 258, 266, 268, 269, 270 and 273 of SEQ IDNO:1, wherein said amino acid residues to be substituted are selected bycomparing a crystal structure of wild type chalcone synthase of SEQ IDNO:1 with a model structure of the plant polyketide synthase.
 23. Amethod of altering the substrate specificity of a chalcone synthase,said method comprising: (a) substituting one or more amino acids in theactive site of wild type chalcone synthase with one or more amino acidresidues at the corresponding positions in a plant polyketide synthase,wherein said one or more amino acids to be substituted correspond topositions selected from the group consisting of positions 132, 133, 137,161, 194, 197, 211, 216, 254, 256, 263, 265, 267 and 338 of SEQ ID NO:1,thereby producing a chalcone synthase with altered substratespecificity; and (b) testing the substrate specificity of the alteredchalcone synthase and identifying those chalcone synthases havingaltered substrate specificity.
 24. The method of claim 23, wherein thewild type chalcone synthase comprises at least fourteen active siteα-carbons having the structural coordinates of Table 1 (SEQ ID NO:1).25. A method of altering the activity of a chalcone synthase, saidmethod comprising: (a) substituting one or more amino acids in theactive site of wild type chalcone synthase with one or more amino acidresidues at the corresponding positions in a plant polyketide synthase,wherein said one or more amino acids to be substituted correspond topositions selected from the group consisting of positions 96, 98, 99,131, 133, 134, 135, 137, 157, 158, 159, 160, 165, 255, 257, 258, 266,268, 269, 270 and 273 of SEQ ID NO:1, thereby producing a chalconesynthase with altered activity; and (b) testing the activity of thealtered chalcone synthase and identifying those chalcone synthaseshaving altered activity.
 26. The method of claim 25, wherein the wildtype chalcone synthase comprises at least fourteen active site α-carbonshaving the structural coordinates of Table 1 (SEQ ID NO:1).
 27. Themethod of claim 25, wherein said one or more substitutions are selectedfrom the group consisting of D96A, V98L, V99A, T131S, S133T, G134T,V135P, M137L, Y157V, M158G, M159V, Y160F, Q165H, D255G, H257K, L258V,H266Q, L268K, K269G, D270A and G273D.
 28. The method of claim 25,wherein said plant polyketide synthase is a stilbene synthase.
 29. Themethod of claim 25, wherein the altered activity results in theformation of the product of the plant polyketide synthase instead of theproduct of the wild type chalcone synthase.
 30. The method of claim 25,wherein the altered activity results in the formation of both theproduct of the plant polyketide synthase and the product of the wildtype chalcone synthase.
 31. The method of claim 28, wherein the alteredactivity results in the formation of resveratrol instead of chalcone.32. The method of claim 28, wherein the altered activity results in theformation of both resveratrol and chalcone.
 33. A method of altering theactivity of a chalcone synthase, said method comprising: (a)substituting an amino acid in the active site of wild type chalconesynthase with an amino acid residue at the corresponding position in aplant polyketide synthase, wherein said amino acid to be substitutedcorresponds to position 100 of SEQ ID NO:1, thereby producing a chalconesynthase with altered activity; and (b) testing the activity of thealtered chalcone synthase and identifying those chalcone synthaseshaving altered activity.
 34. The method of claim 33, wherein the wildtype chalcone synthase comprises at least fourteen active site α-carbonshaving the structural coordinates of Table 1 (SEQ ID NO:1).
 35. Themethod of claim 33, wherein said substitution is V100M.
 36. The methodof claim 33, wherein said plant polyketide synthase is a stilbenesynthase.
 37. The method of claim 33, wherein the altered activityresults in the formation of the product of the plant polyketide synthaseinstead of the product of the wild type chalcone synthase.
 38. Themethod of claim 33, wherein the altered activity results in theformation of both the product of the plant polyketide synthase and theproduct of the wild type chalcone synthase.
 39. The method of claim 33,wherein the altered activity results in the formation of resveratrolinstead of chalcone.
 40. The method of claim 33, wherein the alteredactivity results in the formation of both resveratrol and chalcone.